9,290 results on '"Holin A"'
Search Results
2. A dimeric holin/antiholin complex controls lysis by phage T4
- Author
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Jan Michel Frederik Schwarzkopf, Denise Mehner-Breitfeld, and Thomas Brüser
- Subjects
protein–protein interaction ,membrane protein ,bacteriophage ,holin ,antiholin ,phage T4 ,Microbiology ,QR1-502 - Abstract
Lytic phages control the timepoint of host cell lysis by timing the holin-mediated release of cell wall-degrading endolysins. In phage T4, the antiholin RI inhibits the holin T, thereby preventing the early release of the T4 endolysin and lysis. The antiholin achieves lysis inhibition (LIN) in response to phage superinfections, thereby increasing the chance for lysis in an environment with a lower phage concentration. The holin T consists of a small N-terminal cytoplasmic domain, a transmembrane helix, and a periplasmic C-terminal domain. The antiholin is targeted to the periplasm by a cleavable signal peptide. Recently, the periplasmic soluble domains of the holin and the antiholin were found to form T2/RI2 tetramers in crystals. To investigate the functional relevance of this complex, we reconstituted LIN in a phage-free system, using only RI, T, and endolysin, and combined targeted mutagenesis with functional analyses. Inactivation of the RI signal peptide cleavage site did not abolish LIN, indicating that RI can function in a membrane-bound state, which argued against the tetramer. This led to analyses showing that only one of the two T/RI interfaces in the tetramer is physiologically relevant, which is also the only interaction site predicted by AlphaFold2. Some holin mutations at this interaction site prevented lysis, suggesting that the RI interaction likely acts by blocking the holin oligomerization required for hole formation. We conclude that LIN is mediated by a dimeric T/RI complex that, unlike the tetramer, can be easily formed when both partners are membrane-anchored.
- Published
- 2024
- Full Text
- View/download PDF
3. Co-transcribed genes SA1833-SA1832 promote persister formation by regulating the transcription of holin-like gene lrgA in methicillin-resistant Staphylococcus aureus strain N315
- Author
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Shiwen Xu, Jiade Zhu, Yujie Li, and Baolin Sun
- Subjects
Staphylococcus aureus ,Toxin proteins ,Persister formation ,Ceftizoxime ,Holin-like gene lrgA ,Microbiology ,QR1-502 ,Other systems of medicine ,RZ201-999 - Abstract
Staphylococcus aureus, a facultative anaerobic gram-positive bacterial pathogen, has posed major threat to public health worldwide. Upon S. aureus infection, the host immune system is activated for clearance. However, intracellular S. aureus, which remains viable for an extended time, has evolved the ability to escape from immune response and extracellular antibiotics. One of possible strategies is the formation of persisters. Persistence is one of the major causes of S. aureus relapse infection but the underlying mechanisms remain obscure. Here, we identified two co-transcribed genes SA1833-SA1832 that are involved in persister formation in S. aureus. Dysfunction of SA1833 and/or SA1832 significantly reduces persister formation in the presence of ceftizoxime. Additionally, we found that the expression of SA1833 and SA1832 under the induction of oxidative stress and SOS response is strictly regulated by the LexA-RecA pathway. Interestingly, SA1833-SA1832 contributes to persister formation in an lrgA-dependent manner. Moreover, the mouse RAW264.7 macrophage infection model indicated that disrupting SA1833-SA1832 inhibits S. aureus from infecting macrophages and impairs its ability to survive in the intracellular environment.
- Published
- 2024
- Full Text
- View/download PDF
4. Co-transcribed genes SA1833-SA1832 promote persister formation by regulating the transcription of holin-like gene lrgA in methicillin-resistant Staphylococcus aureus strain N315
- Author
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Xu, Shiwen, Zhu, Jiade, Li, Yujie, and Sun, Baolin
- Published
- 2024
- Full Text
- View/download PDF
5. Elucidating Physicochemical Features of Holin Proteins Responsible for Bacterial Cell Lysis.
- Author
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Mondal, Anupam, Teimouri, Hamid, and Kolomeisky, Anatoly B.
- Published
- 2024
- Full Text
- View/download PDF
6. Prediction and identification of new type holin protein of Escherichia coli phage ECP26
- Author
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Park, Do-Won, Lee, Jong Hun, and Park, Jong-Hyun
- Published
- 2022
- Full Text
- View/download PDF
7. A GH19 lysozyme and peptidase from Myoviridae cyanophages lacking the typical holin-endolysin system exhibit lytic activity
- Author
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Meng, Li-Hui, Ke, Fei, Zhang, Qi-Ya, Hu, Ya-Dong, and Zhao, Zhe
- Published
- 2024
- Full Text
- View/download PDF
8. A novel holin from an Enterococcus faecalis phage and application in vitro and in vivo
- Author
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Xiang, Yingying, Wang, Suping, Huang, Hao, Li, Xuelin, Li, Haiyan, Tu, Yungui, Wei, Yunlin, Song, Fei, and Ji, Xiuling
- Published
- 2024
- Full Text
- View/download PDF
9. Sensitive detection of viable Cronobacter sakazakii by bioluminescent reporter phage emitting stable signals with truncated holin
- Author
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Kim, Doyeon and Kim, Minsik
- Published
- 2023
- Full Text
- View/download PDF
10. A dimeric holin/antiholin complex controls lysis by phage T4.
- Author
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Schwarzkopf, Jan Michel Frederik, Mehner-Breitfeld, Denise, and Brüser, Thomas
- Subjects
BACTERIOPHAGE T4 ,CD4 antigen ,MEMBRANE proteins ,PEPTIDES ,LYSIS - Abstract
Lytic phages control the timepoint of host cell lysis by timing the holin-mediated release of cell wall-degrading endolysins. In phage T4, the antiholin RI inhibits the holin T, thereby preventing the early release of the T4 endolysin and lysis. The antiholin achieves lysis inhibition (LIN) in response to phage superinfections, thereby increasing the chance for lysis in an environment with a lower phage concentration. The holin T consists of a small N-terminal cytoplasmic domain, a transmembrane helix, and a periplasmic C-terminal domain. The antiholin is targeted to the periplasm by a cleavable signal peptide. Recently, the periplasmic soluble domains of the holin and the antiholin were found to form T
2 /RI2 tetramers in crystals. To investigate the functional relevance of this complex, we reconstituted LIN in a phage-free system, using only RI, T, and endolysin, and combined targeted mutagenesis with functional analyses. Inactivation of the RI signal peptide cleavage site did not abolish LIN, indicating that RI can function in a membrane-bound state, which argued against the tetramer. This led to analyses showing that only one of the two T/RI interfaces in the tetramer is physiologically relevant, which is also the only interaction site predicted by AlphaFold2. Some holin mutations at this interaction site prevented lysis, suggesting that the RI interaction likely acts by blocking the holin oligomerization required for hole formation. We conclude that LIN is mediated by a dimeric T/RI complex that, unlike the tetramer, can be easily formed when both partners are membrane-anchored. [ABSTRACT FROM AUTHOR]- Published
- 2024
- Full Text
- View/download PDF
11. Computational Simulation of Holin S105 in Membrane Bilayer and Its Dimerization Through a Helix-Turn-Helix Motif
- Author
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Zhou, Brian, Wu, Yinghao, and Su, Zhaoqian
- Published
- 2021
- Full Text
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12. Characterization of a lytic Pseudomonas aeruginosa phage vB_PaeP_ASP23 and functional analysis of its lysin LysASP and holin HolASP
- Author
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Jiaqi Cui, Xiaojie Shi, Xinwei Wang, Huzhi Sun, Yanxin Yan, Feiyang Zhao, Can Zhang, Wenhua Liu, Ling Zou, Lei Han, Qiang Pan, and Huiying Ren
- Subjects
Pseudomonas aeruginosa phage ,genome analysis ,lysin ,holin ,gene expression ,phage display technology ,Microbiology ,QR1-502 - Abstract
In this study, we isolated a lytic Pseudomonas aeruginosa phage (vB_PaeP_ASP23) from the sewage of a mink farm, characterized its complete genome and analyzed the function of its putative lysin and holin. Morphological characterization and genome annotation showed that phage ASP23 belonged to the Krylovirinae family genus Phikmvvirus, and it had a latent period of 10 min and a burst size of 140 pfu/infected cell. In minks challenged with P. aeruginosa, phage ASP23 significantly reduced bacterial counts in the liver, lung, and blood. The whole-genome sequencing showed that its genome was a 42,735-bp linear and double-stranded DNA (dsDNA), with a G + C content of 62.15%. Its genome contained 54 predicted open reading frames (ORFs), 25 of which had known functions. The lysin of phage ASP23 (LysASP), in combination with EDTA, showed high lytic activity against P. aeruginosa L64. The holin of phage ASP23 was synthesized by M13 phage display technology, to produce recombinant phages (HolASP). Though HolASP exhibited a narrow lytic spectrum, it was effective against Staphylococcus aureus and Bacillus subtilis. However, these two bacteria were insensitive to LysASP. The findings highlight the potential of phage ASP23 to be used in the development of new antibacterial agents.
- Published
- 2023
- Full Text
- View/download PDF
13. Topological examination of the bacteriophage lambda S holin by EPR spectroscopy
- Author
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Morris, Andrew K., Perera, Rehani S., Sahu, Indra D., and Lorigan, Gary A.
- Published
- 2023
- Full Text
- View/download PDF
14. Spatial and temporal control of lysis by the lambda holin
- Author
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Jesse Cahill, Ashley Holt, Matthew Theodore, Russell Moreland, Chandler O'Leary, Cody Martin, Kelsey Bettridge, Jie Xiao, and Ry Young
- Subjects
holes ,rafts ,lysis ,polar ,thioflavin-T ,plasmolysis ,Microbiology ,QR1-502 - Abstract
ABSTRACT The infection cycle of phage λ terminates in lysis mediated by three types of lysis proteins, each disrupting a layer in the bacterial envelope: the S105 holin, the R endolysin, and the Rz/Rz1 spanin complex targeting the inner membrane, cell wall or peptidoglycan, and the outer membrane, respectively. Video microscopy has shown that in most infections, lysis occurs as a sudden, explosive event at a cell pole, such that the initial product is a less refractile ghost that retains rod-shaped morphology. Here, we investigate the molecular basis of polar lysis using time-lapse fluorescence microscopy. The results indicate that the holin determines the morphology of lysis by suddenly forming two-dimensional rafts at the poles about 100 s prior to lysis. Given the physiological and biochemical similarities between the lambda holin and other class I holins, dynamic redistribution and sudden concentration may be common features of holins, probably reflecting the fitness advantage of all-or-nothing lysis regulation.IMPORTANCEIn this study, we use fluorescent video microscopy to track -green fluorescent protein (GFP)-labeled holin in the minutes prior to phage lysis. Our work contextualizes prior genetic and biochemical data, showing when hole formation starts and where holin oligomers form in relation to the site of lytic rupture. Furthermore, prior work showed that the morphology of lambda-infected cells is characterized by an explosive event starting at the cell pole; however, the basis for this was not clear. This study shows that holin most often oligomerizes at cell poles and that the site of the oligomerization is spatially correlated with the site of lytic blowout. Therefore, the holin is the key contributor to polar lysis morphology for phage lambda.
- Published
- 2024
- Full Text
- View/download PDF
15. Functional Analysis of the Endopeptidase and Holin From Planktothrix agardhii Cyanophage PaV-LD
- Author
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Li-Hui Meng, Fei Ke, Qi-Ya Zhang, and Zhe Zhao
- Subjects
Planktothrix agardhii ,cyanophage PaV-LD ,endopeptidase ,holin ,Synechocystis sp. PCC6803 ,Microbiology ,QR1-502 - Abstract
A cyanophage PaV-LD, previously isolated from harmful filamentous cyanobacterium Planktothrix agardhii, was sequenced, and co-expression of its two ORFs in tandem, ORF123 and ORF124, inhibited growth on the model cyanobacterium Synechocystis sp. PCC6803 cells. However, the mechanism of action of ORF123 and ORF124 alone remains to be elucidated. In this study, we aimed to study the individual function of ORF123 or ORF124 from PaV-LD. Our data showed that the ORF123 encoded an endopeptidase, which harbored an M23 family peptidase domain and a transmembrane region. The expression of the endopeptidase in Escherichia coli alone revealed that the protein exhibited remarkable bacteriostatic activity, as evidenced by observation of growth inhibition, membrane damage, and leakage of the intracellular enzyme. Similarly, the holin, a membrane-associated protein encoded by the ORF124, showed weak bacteriostatic activity on E. coli. Moreover, deletion mutations indicated that the transmembrane domains of endopeptidase and holin were indispensable for their bacteriostatic activity. Meanwhile, the bacteriostatic functions of endopeptidase and holin on cyanobacteria cells were confirmed by expressing them in the cyanobacterium Synechocystis sp. PCC6803. Collectively, our study revealed the individual role of endopeptidase or holin and their synergistic bacteriolytic effect, which would contribute to a better understanding of the lytic mechanism of cyanophage PaV-LD.
- Published
- 2022
- Full Text
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16. SAS HOLIN secures contract for Building Alteration Work - Covering - Waterproofing
- Subjects
Contract agreement ,News, opinion and commentary - Abstract
France based SAS HOLIN has secured contract from Mairie de Fresnes-sur-Escaut for Building Alteration Work - Covering - Waterproofing. The value of the contract is worth 136057.37 EUR. Copyright © [...]
- Published
- 2024
17. Cloning and expression analysis of fused holin-endolysin from RL bacteriophage; Exhibits broad activity against multi drug resistant pathogens
- Author
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Basit, Abdul, Qadir, Sania, Qureshi, Sara, and Rehman, Shafiq Ur
- Published
- 2021
- Full Text
- View/download PDF
18. Occurrence and potential mechanism of holin-mediated non-lytic protein translocation in bacteria
- Author
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Thomas Brüser and Denise Mehner-Breitfeld
- Subjects
holins ,endolysins ,toxins ,tat transport ,bacteriocins ,clostridia ,Biology (General) ,QH301-705.5 - Abstract
Holins are generally believed to generate large membrane lesions that permit the passage of endolysins across the cytoplasmic membrane of prokaryotes, ultimately resulting in cell wall degradation and cell lysis. However, there are more and more examples known for non-lytic holin-dependent secretion of proteins by bacteria, indicating that holins somehow can transport proteins without causing large membrane lesions. Phage-derived holins can be used for a non-lytic endolysin translocation to permeabilize the cell wall for the passage of secreted proteins. In addition, clostridia, which do not possess the Tat pathway for transport of folded proteins, most likely employ non-lytic holin-mediated transport also for secretion of toxins and bacteriocins that are incompatible with the general Sec pathway. The mechanism for non-lytic holin-mediated transport is unknown, but the recent finding that the small holin TpeE mediates a non-lytic toxin secretion in Clostridium perfringens opened new perspectives. TpeE contains only one short transmembrane helix that is followed by an amphipathic helix, which is reminiscent of TatA, the membrane-permeabilizing component of the Tat translocon for folded proteins. Here we review the known cases of non-lytic holin-mediated transport and then focus on the structural and functional comparison of TatA and TpeE, resulting in a mechanistic model for holin-mediated transport. This model is strongly supported by a so far not recognized naturally occurring holin-endolysin fusion protein.
- Published
- 2022
- Full Text
- View/download PDF
19. Getting Outside the Cell: Versatile Holin Strategies Used by Distinct Phages to Leave Their Bacillus thuringiensis Host
- Author
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UCL - SST/ELI/ELIM - Applied Microbiology, Leprince, Audrey, Nuytten, Manon, July, Elise, Tesseur, Coralie, Mahillon, Jacques, UCL - SST/ELI/ELIM - Applied Microbiology, Leprince, Audrey, Nuytten, Manon, July, Elise, Tesseur, Coralie, and Mahillon, Jacques
- Abstract
Holins are small transmembrane proteins involved in the final stage of the lytic cycle of double-stranded DNA (dsDNA) phages. They cooperate with endolysins to achieve bacterial lysis, thereby releasing the phage progeny into the extracellular environment. Besides their role as membrane permeabilizers, allowing endolysin transfer and/or activation, holins also regulate the lysis timing. In this work, we provide functional characterization of the holins encoded by three phages targeting the Bacillus cereus group. The siphovirus Deep-Purple has a lysis cassette in which holP30 and holP33 encode two proteins displaying holin properties, including a transmembrane domain. The holin genes were expressed in Escherichia coli and induced bacterial lysis, with HolP30 being more toxic than HolP33. In Bacillus thuringiensis, the simultaneous expression of both holins was necessary to observe lysis, suggesting that they may interact to form functional pores. The myoviruses Deep-Blue and Vp4 both encode a single candidate holin (HolB and HolV, respectively) with two transmembrane domains, whose genes are not located near the endolysin genes. Their function as holin proteins was confirmed as their expression in E. coli impaired cell growth and viability. The HolV expression in B. thuringiensis also led to bacterial lysis, which was enhanced by coexpressing the holin with its cognate endolysin. Despite similar organizations and predicted topologies, truncated mutants of the HolB and HolV proteins showed different toxicity levels, suggesting that differences in amino acid composition influence their lysis properties.
- Published
- 2022
20. Biological Characterization and Evolution of Bacteriophage T7-△holin During the Serial Passage Process
- Author
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Hai Xu, Xi Bao, Weiming Hong, Anping Wang, Kaimin Wang, Hongyan Dong, Jibo Hou, Roshini Govinden, Bihua Deng, and Hafizah Y. Chenia
- Subjects
T7 phage ,holin ,lysis ,compensatory host ,evolution ,Microbiology ,QR1-502 - Abstract
Bacteriophage T7 gene 17.5 coding for the only known holin is one of the components of its lysis system, but the holin activity in T7 is more complex than a single gene, and evidence points to the existence of additional T7 genes with holin activity. In this study, a T7 phage with a gene 17.5 deletion (T7-△holin) was rescued and its biological characteristics and effect on cell lysis were determined. Furthermore, the genomic evolution of mutant phage T7-△holin during serial passage was assessed by whole-genome sequencing analysis. It was observed that deletion of gene 17.5 from phage T7 delays lysis time and enlarges the phage burst size; however, this biological characteristic recovered to normal lysis levels during serial passage. Scanning electron microscopy showed that the two opposite ends of E. coli BL21 cells swell post-T7-△holin infection rather than drilling holes on cell membrane when compared with T7 wild-type infection. No visible progeny phage particle accumulation was observed inside the E. coli BL21 cells by transmission electron microscopy. Following serial passage of T7-△holin from the 1st to 20th generations, the mRNA levels of gene 3.5 and gene 19.5 were upregulated and several mutation sites were discovered, especially two missense mutations in gene 19.5, which indicate a potential contribution to the evolution of the T7-△holin. Although the burst size of T7-△holin increased, high titer cultivation of T7-△holin was not achieved by optimizing the culture process. Accordingly, these results suggest that gene 19.5 is a potential lysis-related component that needs to be studied further and that the T7-△holin strain with its gene 17.5 deletion is not adequate to establish the high-titer phage cultivation process.
- Published
- 2021
- Full Text
- View/download PDF
21. Extracellular vesicle formation in Lactococcus lactis is stimulated by prophage‐encoded holin–lysin system
- Author
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Yue Liu, Marcel H. Tempelaars, Sjef Boeren, Svetlana Alexeeva, Eddy J. Smid, and Tjakko Abee
- Subjects
Biotechnology ,TP248.13-248.65 - Abstract
Summary Gram‐positive bacterial extracellular membrane vesicles (EVs) have been drawing more attention in recent years. However, mechanistic insights are still lacking on how EVs are released through the cell walls in Gram‐positive bacteria. In this study, we characterized underlying mechanisms of EV production and provide evidence for a role of prophage activation in EV release using the Gram‐positive bacterium Lactococcus lactis as a model. By applying a standard EV isolation procedure, we observed the presence of EVs in the culture supernatant of a lysogenic L. lactis strain FM‐YL11, for which the prophage‐inducing condition led to an over 10‐fold increase in EV production in comparison with the non‐inducing condition. In contrast, the prophage‐encoded holin–lysin knockout mutant YL11ΔHLH and the prophage‐cured mutant FM‐YL12 produced constantly low levels of EVs. Under the prophage‐inducing condition, FM‐YL11 did not show massive cell lysis. Defective phage particles were found to be released in and associated with holin–lysin‐induced EVs from FM‐YL11, as demonstrated by transmission electron microscopic images, flow cytometry and proteomics analysis. Findings from this study further generalized the EV‐producing phenotype to Gram‐positive L. lactis, and provide additional insights into the EV production mechanism involving prophage‐encoded holin–lysin system. The knowledge on bacterial EV production can be applied to all Gram‐positive bacteria and other lactic acid bacteria with important roles in fermentations and probiotic formulations, to enable desired release and delivery of cellular components with nutritional values or probiotic effects.
- Published
- 2022
- Full Text
- View/download PDF
22. Occurrence and potential mechanism of holin-mediated non-lytic protein translocation in bacteria
- Author
-
Brüser, Thomas, Mehner-Breitfeld, Denise, Brüser, Thomas, and Mehner-Breitfeld, Denise
- Abstract
Holins are generally believed to generate large membrane lesions that permit the passage of endolysins across the cytoplasmic membrane of prokaryotes, ultimately resulting in cell wall degradation and cell lysis. However, there are more and more examples known for non-lytic holin-dependent secretion of proteins by bacteria, indicating that holins somehow can transport proteins without causing large membrane lesions. Phage-derived holins can be used for a non-lytic endolysin translocation to permeabilize the cell wall for the passage of secreted proteins. In addition, clostridia, which do not possess the Tat pathway for transport of folded proteins, most likely employ non-lytic holin-mediated transport also for secretion of toxins and bacteriocins that are incompatible with the general Sec pathway. The mechanism for non-lytic holin-mediated transport is unknown, but the recent finding that the small holin TpeE mediates a non-lytic toxin secretion in Clostridium perfringens opened new perspectives. TpeE contains only one short transmembrane helix that is followed by an amphipathic helix, which is reminiscent of TatA, the membrane-permeabilizing component of the Tat translocon for folded proteins. Here we review the known cases of non-lytic holin-mediated transport and then focus on the structural and functional comparison of TatA and TpeE, resulting in a mechanistic model for holin-mediated transport. This model is strongly supported by a so far not recognized naturally occurring holin-endolysin fusion protein.
- Published
- 2022
23. Ekstrakcija fenolnih jedinjenja iz propolisa primenom prirodnih eutektičkih smeša na bazi holin-hlorida, prolina i glicina
- Author
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Jovanović, Dijana D. and Jovanović, Dijana D.
- Abstract
Eutektičke smeše su smeše čija je temperatura topljenja niža nego temperatura topljenja pojedinačnih komponenti koje je izgrađuju. Primarni biljni metaboliti grade eutektičke smeše koje „imitiraju ekstracelularnu tečnost u biljkama” u kojoj su rastvoreni sekundarni metaboliti, zbog čega su i našli primenu kao zeleni i prirodni rastvarači. U ovom radu analizirana je efikasnost ekstrakcije fenolnih jedinjenja iz propolisa primenom 29 različitih eutektičkih smeša. Fenolni profili ekstrakata analizirani su visokoefikasnom tankoslojnom hromatografijom. Postupak ekstrakcije i hemijske karakterizacije je optimizovan. Efikasnost ekstrakcije eutektičkim smešama procenjena je poređenjem sa konvencionalnim organskim rastvaračima. Ekstrakti su se grupisali prema tipu rastvarača, a zone najodgovornije za grupisanje su identifikovane. Eutektičke smeše holin hlorida sa glicerolom i vinskom kiselinom ekstrahovale su sličnu količinu fenolnih jedinjenja iz propolisa, dok su eutektičke smeše holin hlorida sa ureom i mlečnom kiselinom ekstrahovale različitu količinu fenolnih jedinjenja od gore pomenutih smeša.
- Published
- 2022
24. Ultrasound assisted extraction of pectin from waste apple pomace using choline chloride based eutectic solvents
- Author
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Pantić, Olga, Spasojević, Pavle, Panić, Vesna, Marković, Maja D., Savić, Sanja I., Kalagasidis Krušić, Melina, Pantić, Olga, Spasojević, Pavle, Panić, Vesna, Marković, Maja D., Savić, Sanja I., and Kalagasidis Krušić, Melina
- Abstract
Pectin and pectin derived oligosaccharides can be obtained from waste apple pomace(biomass). Traditional method for pectin extraction involves use of diluted mineral acids atelevated temperatures, with yields of about 10 to 15%. As an alternative to conventionalmethods, the use of eutectic solvents is increasing because of their superior propertieswhen it comes to targeted extraction of certain components from biomass. The aim of thispaper is ultrasound assisted extraction of pectin from waste apple pomace using cholinechloride based eutectic solvents and lactic acid. Properties of extracted products wereexamined using FTIR spectroscopy and differential scanning calorimetry., Pektin i pektinski oligosaharidi mogu se dobiti iz otpadne jabučne kaše. Ovaj prirodni polimer ima široku primenu u industriji. Tradicionalna metoda za ekstrakciju pektina podrazumeva tretman razblaženim mineralnim kiselinama na povišenoj temperaturi, pri čemu se prinosi ostvaruju od oko 10 do 15%. Kao alternativa tradicionalnim rastvaračima sve češće se koriste i eutektički rastvarači, koje odlikuju daleko superiornija svojstva kada je reč o ciljanoj ekstrakciji određenih komponenti iz biomase. Cilj ovog rada je ultrazvučna ekstrakcija pektina primenom eutektičkih rastvarača na bazi holin hlorida i mlečne kiseline. Svojstva ekstrahovanog proizvoda ispitana su primenom FTIR spektroskopije i diferencijalne skenirajuće kalorimetrije.
- Published
- 2022
25. Topological and phylogenetic analyses of bacterial holin families and superfamilies
- Author
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Reddy, Bhaskara L and Saier, Milton H
- Subjects
Biochemistry and Cell Biology ,Biological Sciences ,Amino Acid Sequence ,Bacteria ,Bacterial Proteins ,Membrane Proteins ,Molecular Sequence Data ,Phylogeny ,Sequence Homology ,Amino Acid ,Holin ,"Hole-forming" ,Transmembrane pore ,Autolysin ,Superfamily ,“Hole-forming” ,Physical Sciences ,Biological sciences ,Physical sciences - Abstract
Holins are small "hole-forming" transmembrane proteins that mediate bacterial cell lysis during programmed cell death or following phage infection. We have identified fifty two families of established or putative holins and have included representative members of these proteins in the Transporter Classification Database (TCDB; www.tcdb.org). We have identified the organismal sources of members of these families, calculated their average protein sizes, estimated their topologies and determined their relative family sizes. Topological analyses suggest that these proteins can have 1, 2, 3 or 4 transmembrane α-helical segments (TMSs), and members of a single family are frequently, but not always, of a single topology. In one case, proteins of a family proved to have either 2 or 4 TMSs, and the latter arose by intragenic duplication of a primordial 2 TMS protein-encoding gene resembling the former. Using established statistical approaches, some of these families have been shown to be related by common descent. Seven superfamilies, including 21 of the 52 recognized families were identified. Conserved motif and Pfam analyses confirmed most superfamily assignments. These results serve to expand upon the scope of channel-forming bacterial holins.
- Published
- 2013
26. Identification and Characterization of a New Type of Holin-Endolysin Lysis Cassette in Acidovorax oryzae Phage AP1
- Author
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Muchen Zhang, Yanli Wang, Jie Chen, Xianxian Hong, Xinyan Xu, Zhifeng Wu, Temoor Ahmed, Belinda Loh, Sebastian Leptihn, Sabry Hassan, Mohamed M. Hassan, Guochang Sun, and Bin Li
- Subjects
Acidovorax oryzae phage AP1 ,lysis cassette ,holin ,endolysin ,Microbiology ,QR1-502 - Abstract
Phages utilize lysis systems to allow the release of newly assembled viral particles that kill the bacterial host. This is also the case for phage AP1, which infects the rice pathogen Acidovorax oryzae. However, how lysis occurs on a molecular level is currently unknown. We performed in silico bioinformatics analyses, which indicated that the lysis cassette contains a holin (HolAP) and endolysin (LysAP), which are encoded by two adjacent genes. Recombinant expression of LysAP caused Escherichia coli lysis, while HolAP arrested growth. Co-expression of both proteins resulted in enhanced lysis activity compared to the individual proteins alone. Interestingly, LysAP contains a C-terminal region transmembrane domain, which is different from most known endolysins where a N-terminal hydrophobic region is found, with the potential to insert into the membrane. We show that the C-terminal transmembrane domain is crucial for protein localization and bacterial lysis in phage AP1. Our study characterizes the new phage lysis cassette and the mechanism to induce cell disruption, giving new insight in the understanding of phage life cycles.
- Published
- 2022
- Full Text
- View/download PDF
27. The Holin-Endolysin Lysis System of the OP2-Like Phage X2 Infecting Xanthomonas oryzae pv. oryzae
- Author
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Zhifeng Wu, Yang Zhang, Xinyang Xu, Temoor Ahmed, Yong Yang, Belinda Loh, Sebastian Leptihn, Chenqi Yan, Jianping Chen, and Bin Li
- Subjects
transmembrane domain ,endolysin ,holin ,morphological change ,lysis ,phage ,Microbiology ,QR1-502 - Abstract
Most endolysins of dsDNA phages are exported by a holin-dependent mechanism, while in some cases endolysins are exported via a holin-independent mechanism. However, it is still unclear whether the same endolysins can be exported by both holin-dependent and holin-independent mechanisms. This study investigated the lysis system of OP2-like phage X2 infecting Xanthomonas oryzae pv. oryzae, causing devastating bacterial leaf blight disease in rice. Based on bioinformatics and protein biochemistry methods, we show that phage X2 employs the classic "holin-endolysin" lysis system. The endolysin acts on the cell envelope and exhibits antibacterial effects in vitro, while the holin facilitates the release of the protein into the periplasm. We also characterized the role of the transmembrane domain (TMD) in the translocation of the endolysin across the inner membrane. We found that the TMD facilitated the translocation of the endolysin via the Sec secretion system. The holin increases the efficiency of protein release, leading to faster and more efficient lysis. Interestingly, in E. coli, the expression of either holin or endolysin with TMDs resulted in the formation of long rod shaped cells. We conclude that the TMD of X2-Lys plays a dual role: One is the transmembrane transport while the other is the inhibition of cell division, resulting in larger cells and thus in a higher number of released viruses per cell.
- Published
- 2021
- Full Text
- View/download PDF
28. Search for proton decay via $p\rightarrow{e^+\eta}$ and $p\rightarrow{\mu^+\eta}$ with a 0.37 Mton-year exposure of Super-Kamiokande
- Author
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Collaboration, Super-Kamiokande, Taniuchi, N., Abe, K., Abe, S., Asaoka, Y., Bronner, C., Harada, M., Hayato, Y., Hiraide, K., Hosokawa, K., Ieki, K., Ikeda, M., Kameda, J., Kanemura, Y., Kaneshima, R., Kashiwagi, Y., Kataoka, Y., Miki, S., Mine, S., Miura, M., Moriyama, S., Nakahata, M., Nakayama, S., Noguchi, Y., Pronost, G., Okamoto, K., Sato, K., Sekiya, H., Shiba, H., Shimizu, K., Shiozawa, M., Sonoda, Y., Suzuki, Y., Takeda, A., Takemoto, Y., Takenaka, A., Tanaka, H., Watanabe, S., Yano, T., Kajita, T., Okumura, K., Tashiro, T., Tomiya, T., Wang, X., Yoshida, S., Megias, G. D., Fernandez, P., Labarga, L., Ospina, N., Zaldivar, B., Pointon, B. W., Kearns, E., Mirabito, J., Raaf, J. L., Wan, L., Wester, T., Bian, J., Griskevich, N. J., Kropp, W. R., Locke, S., Smy, M. B., Sobel, H. W., Takhistov, V., Yankelevich, A., Hill, J., Jang, M. C., Kim, J. Y., Lee, S. H., Lim, I. T., Moon, D. H., Park, R. G., Yang, B. S., Bodur, B., Scholberg, K., Walter, C. W., Beauchêne, A., Bernard, L., Coffani, A., Drapier, O., Hedri, S. El, Giampaolo, A., Mueller, Th. A., Santos, A. D., Paganini, P., Rogly, R., Nakamura, T., Jang, J. S., Machado, L. N., Learned, J. G., Choi, K., Iovine, N., Cao, S., Anthony, L. H. V., Martin, D., Prouse, N. W., Scott, M., Sztuc, A. A., Uchida, Y., Berardi, V., Calabria, N. F., Catanesi, M. G., Radicioni, E., Langella, A., De Rosa, G., Collazuol, G., Feltre, M., Iacob, F., Lamoureux, M., Mattiazzi, M., Ludovici, L., Gonin, M., Périssé, L., Quilain, B., Fujisawa, C., Horiuchi, S., Kobayashi, M., Liu, Y. M., Maekawa, Y., Nishimura, Y., Okazaki, R., Akutsu, R., Friend, M., Hasegawa, T., Ishida, T., Kobayashi, T., Jakkapu, M., Matsubara, T., Nakadaira, T., Nakamura, K., Oyama, Y., Yrey, A. Portocarrero, Sakashita, K., Sekiguchi, T., Tsukamoto, T., Bhuiyan, N., Boschi, T., Burton, G. T., Di Lodovico, F., Gao, J., Goldsack, A., Katori, T., Migenda, J., Ramsden, R. M., Taani, M., Xie, Z., Zsoldos, S., Kotsar, Y., Ozaki, H., Suzuki, A. T., Takagi, Y., Takeuchi, Y., Yamamoto, S., Zhong, H., Feng, J., Feng, L., Han, S., Hu, J. R., Hu, Z., Kawaue, M., Kikawa, T., Mori, M., Nakaya, T., Wendell, R. A., Yasutome, K., Jenkins, S. J., McCauley, N., Mehta, P., Tarrant, A., Wilking, M. J., Fukuda, Y., Itow, Y., Menjo, H., Ninomiya, K., Yoshioka, Y., Lagoda, J., Mandal, M., Mijakowski, P., Prabhu, Y. S., Zalipska, J., Jia, M., Jiang, J., Jung, C. K., Shi, W., Yanagisawa, C., Hino, Y., Ishino, H., Ito, S., Kitagawa, H., Koshio, Y., Ma, W., Nakanishi, F., Sakai, S., Tada, T., Tano, T., Ishizuka, T., Barr, G., Barrow, D., Cook, L., Samani, S., Wark, D., Holin, A., Nova, F., Jung, S., Yang, J. Y., Yoo, J., Fannon, J. E. P., Kneale, L., Malek, M., McElwee, J. M., Stone, O., Stowell, P., Thiesse, M. D., Thompson, L. F., Wilson, S. T., Okazawa, H., Lakshmi, S. M., Kim, S. B., Kwon, E., Lee, M. W., Seo, J. W., Yu, I., Ichikawa, A. K., Nakamura, K. D., Tairafune, S., Nishijima, K., Koshiba, M., Eguchi, A., Goto, S., Iwamoto, K., Mizuno, Y., Muro, T., Nakagiri, K., Nakajima, Y., Shima, S., Watanabe, E., Yokoyama, M., de Perio, P., Fujita, S., Jesús-Valls, C., Martens, K., Marti, Ll., Tsui, K. M., Vagins, M. R., Xia, J., Izumiyama, S., Kuze, M., Matsumoto, R., Terada, K., Asaka, R., Inomoto, M., Ishitsuka, M., Ito, H., Kinoshita, T., Ommura, Y., Shigeta, N., Shinoki, M., Suganuma, T., Yamauchi, K., Yoshida, T., Nakano, Y., Martin, J. F., Tanaka, H. A., Towstego, T., Gaur, R., Gousy-Leblanc, V., Hartz, M., Konaka, A., Li, X., Chen, S., Wu, Y., Xu, B. D., Zhang, A. Q., Zhang, B., Posiadala-Zezula, M., Boyd, S. B., Edwards, R., Hadley, D., Nicholson, M., O'Flaherty, M., Richards, B., Ali, A., Jamieson, B., Amanai, S., Minamino, A., Pintaudi, G., Sano, S., Sasaki, R., Shibayama, R., Shimamura, R., Suzuki, S., and Wada, K.
- Subjects
High Energy Physics - Experiment - Abstract
A search for proton decay into $e^+/\mu^+$ and a $\eta$ meson has been performed using data from a 0.373 Mton$\cdot$year exposure (6050.3 live days) of Super-Kamiokande. Compared to previous searches this work introduces an improved model of the intranuclear $\eta$ interaction cross section, resulting in a factor of two reduction in uncertainties from this source and $\sim$10\% increase in signal efficiency. No significant data excess was found above the expected number of atmospheric neutrino background events resulting in no indication of proton decay into either mode. Lower limits on the proton partial lifetime of $1.4\times\mathrm{10^{34}~years}$ for $p\rightarrow e^+\eta$ and $7.3\times\mathrm{10^{33}~years}$ for $p\rightarrow \mu^+\eta$ at the 90$\%$ C.L. were set. These limits are around 1.5 times longer than our previous study and are the most stringent to date.
- Published
- 2024
29. The hypothetical track-length fitting algorithm for energy measurement in liquid argon TPCs
- Author
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DUNE Collaboration, Abud, A. Abed, Abi, B., Acciarri, R., Acero, M. A., Adames, M. R., Adamov, G., Adamowski, M., Adams, D., Adinolfi, M., Adriano, C., Aduszkiewicz, A., Aguilar, J., Akbar, F., Alex, N. S., Allison, K., Monsalve, S. Alonso, Alrashed, M., Alton, A., Alvarez, R., Alves, T., Amar, H., Amedo, P., Anderson, J., Andreopoulos, C., Andreotti, M., Andrews, M. P., Andrianala, F., Andringa, S., Anfimov, N., Ankowski, A., Antic, D., Antoniassi, M., Antonova, M., Antoshkin, A., Aranda-Fernandez, A., Arellano, L., Diaz, E. Arrieta, Arroyave, M. A., Asaadi, J., Ashkenazi, A., Asner, D., Asquith, L., Atkin, E., Auguste, D., Aurisano, A., Aushev, V., Autiero, D., Azam, M. B., Azfar, F., Back, A., Back, H., Back, J. J., Bagaturia, I., Bagby, L., Balashov, N., Balasubramanian, S., Baldi, P., Baldini, W., Baldonedo, J., Baller, B., Bambah, B., Banerjee, R., Barao, F., Barbu, D., Barenboim, G., Alzás, P. Barham, Barker, G. J., Barkhouse, W., Barr, G., Monarca, J. Barranco, Barros, A., Barros, N., Barrow, D., Barrow, J. L., Basharina-Freshville, A., Bashyal, A., Basque, V., Batchelor, C., Bathe-Peters, L., Battat, J. B. R., Battisti, F., Bay, F., Bazetto, M. C. Q., Alba, J. L. L. Bazo, Beacom, J. F., Bechetoille, E., Behera, B., Belchior, E., Bell, G., Bellantoni, L., Bellettini, G., Bellini, V., Beltramello, O., Benekos, N., Montiel, C. Benitez, Benjamin, D., Neves, F. Bento, Berger, J., Berkman, S., Bernal, J., Bernardini, P., Bersani, A., Bertolucci, S., Betancourt, M., Rodríguez, A. Betancur, Bevan, A., Bezawada, Y., Bezerra, A. T., Bezerra, T. J., Bhat, A., Bhatnagar, V., Bhatt, J., Bhattacharjee, M., Bhattacharya, M., Bhuller, S., Bhuyan, B., Biagi, S., Bian, J., Biery, K., Bilki, B., Bishai, M., Bitadze, A., Blake, A., Blaszczyk, F. D., Blazey, G. C., Blucher, E., Bodek, A., Bogenschuetz, J., Boissevain, J., Bolognesi, S., Bolton, T., Bomben, L., Bonesini, M., Bonilla-Diaz, C., Bonini, F., Booth, A., Boran, F., Bordoni, S., Merlo, R. Borges, Borkum, A., Bostan, N., Bouet, R., Boza, J., Bracinik, J., Brahma, B., Brailsford, D., Bramati, F., Branca, A., Brandt, A., Bremer, J., Brew, C., Brice, S. J., Brio, V., Brizzolari, C., Bromberg, C., Brooke, J., Bross, A., Brunetti, G., Brunetti, M., Buchanan, N., Budd, H., Buergi, J., Bundock, A., Burgardt, D., Butchart, S., V., G. Caceres, Cagnoli, I., Cai, T., Calabrese, R., Calcutt, J., Calivers, L., Calvo, E., Caminata, A., Camino, A. F., Campanelli, W., Campani, A., Benitez, A. Campos, Canci, N., Capó, J., Caracas, I., Caratelli, D., Carber, D., Carceller, J. M., Carini, G., Carlus, B., Carneiro, M. F., Carniti, P., Terrazas, I. Caro, Carranza, H., Carrara, N., Carroll, L., Carroll, T., Carter, A., Casarejos, E., Casazza, D., Forero, J. F. Castaño, Castaño, F. A., Castillo, A., Castromonte, C., Catano-Mur, E., Cattadori, C., Cavalier, F., Cavanna, F., Centro, S., Cerati, G., Cerna, C., Cervelli, A., Villanueva, A. Cervera, Chakraborty, K., Chalifour, M., Chappell, A., Charitonidis, N., Chatterjee, A., Chen, H., Chen, M., Chen, W. C., Chen, Y., Chen-Wishart, Z., Cherdack, D., Chi, C., Chiapponi, F., Chirco, R., Chitirasreemadam, N., Cho, K., Choate, S., Choi, G., Chokheli, D., Chong, P. S., Chowdhury, B., Christian, D., Chukanov, A., Chung, M., Church, E., Cicala, M. F., Cicerchia, M., Cicero, V., Ciolini, R., Clarke, P., Cline, G., Coan, T. E., Cocco, A. G., Coelho, J. A. B., Cohen, A., Collazo, J., Collot, J., Conley, E., Conrad, J. M., Convery, M., Copello, S., Cova, P., Cox, C., Cremaldi, L., Cremonesi, L., Crespo-Anadón, J. I., Crisler, M., Cristaldo, E., Crnkovic, J., Crone, G., Cross, R., Cudd, A., Cuesta, C., Cui, Y., Curciarello, F., Cussans, D., Dai, J., Dalager, O., Dallavalle, R., Dallaway, W., D'Amico, R., da Motta, H., Dar, Z. A., Darby, R., Peres, L. Da Silva, David, Q., Davies, G. S., Davini, S., Dawson, J., De Aguiar, R., De Almeida, P., Debbins, P., De Bonis, I., Decowski, M. P., de Gouvêa, A., De Holanda, P. C., Astiz, I. L. De Icaza, De Jong, P., Sanchez, P. Del Amo, De la Torre, A., De Lauretis, G., Delbart, A., Delepine, D., Delgado, M., Dell'Acqua, A., Monache, G. Delle, Delmonte, N., De Lurgio, P., Demario, R., De Matteis, G., Neto, J. R. T. de Mello, DeMuth, D. M., Dennis, S., Densham, C., Denton, P., Deptuch, G. W., De Roeck, A., De Romeri, V., Detje, J. P., Devine, J., Dharmapalan, R., Dias, M., Diaz, A., Díaz, J. S., Díaz, F., Di Capua, F., Di Domenico, A., Di Domizio, S., Di Falco, S., Di Giulio, L., Ding, P., Di Noto, L., Diociaiuti, E., Distefano, C., Diurba, R., Diwan, M., Djurcic, Z., Doering, D., Dolan, S., Dolek, F., Dolinski, M. J., Domenici, D., Domine, L., Donati, S., Donon, Y., Doran, S., Douglas, D., Doyle, T. A., Dragone, A., Drielsma, F., Duarte, L., Duchesneau, D., Duffy, K., Dugas, K., Dunne, P., Dutta, B., Duyang, H., Dwyer, D. A., Dyshkant, A. S., Dytman, S., Eads, M., Earle, A., Edayath, S., Edmunds, D., Eisch, J., Englezos, P., Ereditato, A., Erjavec, T., Escobar, C. O., Evans, J. J., Ewart, E., Ezeribe, A. C., Fahey, K., Fajt, L., Falcone, A., Fani', M., Farnese, C., Farrell, S., Farzan, Y., Fedoseev, D., Felix, J., Feng, Y., Fernandez-Martinez, E., Ferry, G., Fialova, E., Fields, L., Filip, P., Filkins, A., Filthaut, F., Fine, R., Fiorillo, G., Fiorini, M., Fogarty, S., Foreman, W., Fowler, J., Franc, J., Francis, K., Franco, D., Franklin, J., Freeman, J., Fried, J., Friedland, A., Fuess, S., Furic, I. K., Furman, K., Furmanski, A. P., Gaba, R., Gabrielli, A., Gago, A. M., Galizzi, F., Gallagher, H., Gallice, N., Galymov, V., Gamberini, E., Gamble, T., Ganacim, F., Gandhi, R., Ganguly, S., Gao, F., Gao, S., Garcia-Gamez, D., García-Peris, M. Á., Gardim, F., Gardiner, S., Gastler, D., Gauch, A., Gauvreau, J., Gauzzi, P., Gazzana, S., Ge, G., Geffroy, N., Gelli, B., Gent, S., Gerlach, L., Ghorbani-Moghaddam, Z., Giammaria, T., Gibin, D., Gil-Botella, I., Gilligan, S., Gioiosa, A., Giovannella, S., Girerd, C., Giri, A. K., Giugliano, C., Giusti, V., Gnani, D., Gogota, O., Gollapinni, S., Gollwitzer, K., Gomes, R. A., Bermeo, L. V. Gomez, Fajardo, L. S. Gomez, Gonnella, F., Gonzalez-Diaz, D., Gonzalez-Lopez, M., Goodman, M. C., Goswami, S., Gotti, C., Goudeau, J., Goudzovski, E., Grace, C., Gramellini, E., Gran, R., Granados, E., Granger, P., Grant, C., Gratieri, D. R., Grauso, G., Green, P., Greenberg, S., Greer, J., Griffith, W. C., Groetschla, F. T., Grzelak, K., Gu, L., Gu, W., Guarino, V., Guarise, M., Guenette, R., Guerzoni, M., Guffanti, D., Guglielmi, A., Guo, B., Guo, F. Y., Gupta, A., Gupta, V., Gurung, G., Gutierrez, D., Guzowski, P., Guzzo, M. M., Gwon, S., Habig, A., Hadavand, H., Haegel, L., Haenni, R., Hagaman, L., Hahn, A., Haiston, J., Hakenmüller, J., Hamernik, T., Hamilton, P., Hancock, J., Happacher, F., Harris, D. A., Hart, A. L., Hartnell, J., Hartnett, T., Harton, J., Hasegawa, T., Hasnip, C. M., Hatcher, R., Hayrapetyan, K., Hays, J., Hazen, E., He, M., Heavey, A., Heeger, K. M., Heise, J., Hellmuth, P., Henry, S., Herner, K., Hewes, V., Higuera, A., Hilgenberg, C., Hillier, S. J., Himmel, A., Hinkle, E., Hirsch, L. R., Ho, J., Hoff, J., Holin, A., Holvey, T., Hoppe, E., Horiuchi, S., Horton-Smith, G. A., Houdy, T., Howard, B., Howell, R., Hristova, I., Hronek, M. S., Huang, J., Huang, R. G., Hulcher, Z., Ibrahim, M., Iles, G., Ilic, N., Iliescu, A. M., Illingworth, R., Ingratta, G., Ioannisian, A., Irwin, B., Isenhower, L., Oliveira, M. Ismerio, Itay, R., Jackson, C. M., Jain, V., James, E., Jang, W., Jargowsky, B., Jena, D., Jentz, I., Ji, X., Jiang, C., Jiang, J., Jiang, L., Jipa, A., Jo, J. H., Joaquim, F. R., Johnson, W., Jollet, C., Jones, B., Jones, R., Jovancevic, N., Judah, M., Jung, C. K., Jung, K. Y., Junk, T., Jwa, Y., Kabirnezhad, M., Kaboth, A. C., Kadenko, I., Kakorin, I., Kalitkina, A., Kalra, D., Kandemir, M., Kaplan, D. M., Karagiorgi, G., Karaman, G., Karcher, A., Karyotakis, Y., Kasai, S., Kasetti, S. P., Kashur, L., Katsioulas, I., Kauther, A., Kazaryan, N., Ke, L., Kearns, E., Keener, P. T., Kelly, K. J., Kemp, E., Kemularia, O., Kermaidic, Y., Ketchum, W., Kettell, S. H., Khabibullin, M., Khan, N., Khvedelidze, A., Kim, D., Kim, J., Kim, M. J., King, B., Kirby, B., Kirby, M., Kish, A., Klein, J., Kleykamp, J., Klustova, A., Kobilarcik, T., Koch, L., Koehler, K., Koerner, L. W., Koh, D. H., Kolupaeva, L., Korablev, D., Kordosky, M., Kosc, T., Kose, U., Kostelecký, V. A., Kothekar, K., Kotler, I., Kovalcuk, M., Kozhukalov, V., Krah, W., Kralik, R., Kramer, M., Kreczko, L., Krennrich, F., Kreslo, I., Kroupova, T., Kubota, S., Kubu, M., Kudenko, Y., Kudryavtsev, V. A., Kufatty, G., Kuhlmann, S., Kulagin, S., Kumar, J., Kumar, P., Kumaran, S., Kunzmann, J., Kuravi, R., Kurita, N., Kuruppu, C., Kus, V., Kutter, T., Kvasnicka, J., Labree, T., Lackey, T., Lalău, I., Lambert, A., Land, B. J., Lane, C. E., Lane, N., Lang, K., Langford, T., Langstaff, M., Lanni, F., Lantwin, O., Larkin, J., Lasorak, P., Last, D., Laudrain, A., Laundrie, A., Laurenti, G., Lavaut, E., Laycock, P., Lazanu, I., LaZur, R., Lazzaroni, M., Le, T., Leardini, S., Learned, J., LeCompte, T., Legin, V., Miotto, G. Lehmann, Lehnert, R., de Oliveira, M. A. Leigui, Leitner, M., Silverio, D. Leon, Lepin, L. M., Li, J. -Y, Li, S. W., Li, Y., Liao, H., Lin, C. S., Lindebaum, D., Linden, S., Lineros, R. A., Lister, A., Littlejohn, B. R., Liu, H., Liu, J., Liu, Y., Lockwitz, S., Lokajicek, M., Lomidze, I., Long, K., Lopes, T. V., Lopez, J., de Rego, I. López, López-March, N., Lord, T., LoSecco, J. M., Louis, W. C., Sanchez, A. Lozano, Lu, X. -G., Luk, K. B., Lunday, B., Luo, X., Luppi, E., MacFarlane, D., Machado, A. A., Machado, P., Macias, C. T., Macier, J. R., MacMahon, M., Maddalena, A., Madera, A., Madigan, P., Magill, S., Magueur, C., Mahn, K., Maio, A., Major, A., Majumdar, K., Mameli, S., Man, M., Mandujano, R. C., Maneira, J., Manly, S., Mann, A., Manolopoulos, K., Plata, M. Manrique, Corchado, S. Manthey, Manyam, V. N., Marchan, M., Marchionni, A., Marciano, W., Marfatia, D., Mariani, C., Maricic, J., Marinho, F., Marino, A. D., Markiewicz, T., Marques, F. Das Chagas, Marquet, C., Marshak, M., Marshall, C. M., Marshall, J., Martina, L., Martín-Albo, J., Martinez, N., Caicedo, D. A. Martinez, López, F. Martínez, Miravé, P. Martínez, Martynenko, S., Mascagna, V., Massari, C., Mastbaum, A., Matichard, F., Matsuno, S., Matteucci, G., Matthews, J., Mauger, C., Mauri, N., Mavrokoridis, K., Mawby, I., Mazza, R., McAskill, T., McConkey, N., McFarland, K. S., McGrew, C., McNab, A., Meazza, L., Meddage, V. C. N., Mefodiev, A., Mehta, B., Mehta, P., Melas, P., Mena, O., Mendez, H., Mendez, P., Méndez, D. P., Menegolli, A., Meng, G., Mercuri, A. C. E. A., Meregaglia, A., Messier, M. D., Metallo, S., Metcalf, W., Mewes, M., Meyer, H., Miao, T., Micallef, J., Miccoli, A., Michna, G., Milincic, R., Miller, F., Miller, G., Miller, W., Mineev, O., Minotti, A., Miralles, L., Mironov, C., Miryala, S., Miscetti, S., Mishra, C. S., Mishra, P., Mishra, S. R., Mislivec, A., Mitchell, M., Mladenov, D., Mocioiu, I., Mogan, A., Moggi, N., Mohanta, R., Mohayai, T. A., Mokhov, N., Molina, J., Bueno, L. Molina, Montagna, E., Montanari, A., Montanari, C., Montanari, D., Montanino, D., Zetina, L. M. Montaño, Mooney, M., Moor, A. F., Moore, Z., Moreno, D., Moreno-Palacios, O., Morescalchi, L., Moretti, D., Moretti, R., Morris, C., Mossey, C., Moura, C. A., Mouster, G., Mu, W., Mualem, L., Mueller, J., Muether, M., Muheim, F., Muir, A., Mukhamejanov, Y., Mulhearn, M., Munford, D., Munteanu, L. J., Muramatsu, H., Muraz, J., Murphy, M., Murphy, T., Muse, J., Mytilinaki, A., Nachtman, J., Nagai, Y., Nagu, S., Nandakumar, R., Naples, D., Narita, S., Navrer-Agasson, A., Nayak, N., Nebot-Guinot, M., Nehm, A., Nelson, J. K., Neogi, O., Nesbit, J., Nessi, M., Newbold, D., Newcomer, M., Nichol, R., Nicolas-Arnaldos, F., Nikolica, A., Nikolov, J., Niner, E., Nishimura, K., Norman, A., Norrick, A., Novella, P., Nowak, A., Nowak, J. A., Oberling, M., Ochoa-Ricoux, J. P., Oh, S., Oh, S. B., Olivier, A., Olshevskiy, A., Olson, T., Onel, Y., Onishchuk, Y., Oranday, A., Osbiston, M., Vélez, J. A. Osorio, O'Sullivan, L., Ormachea, L. Otiniano, Ott, J., Pagani, L., Palacio, G., Palamara, O., Palestini, S., Paley, J. M., Pallavicini, M., Palomares, C., Pan, S., Panda, P., Vazquez, W. Panduro, Pantic, E., Paolone, V., Papaleo, R., Papanestis, A., Papoulias, D., Paramesvaran, S., Paris, A., Parke, S., Parozzi, E., Parsa, S., Parsa, Z., Parveen, S., Parvu, M., Pasciuto, D., Pascoli, S., Pasqualini, L., Pasternak, J., Patrick, C., Patrizii, L., Patterson, R. B., Patzak, T., Paudel, A., Paulucci, L., Pavlovic, Z., Pawloski, G., Payne, D., Pec, V., Pedreschi, E., Peeters, S. J. M., Pellico, W., Perez, A. Pena, Pennacchio, E., Penzo, A., Peres, O. L. G., Gonzalez, Y. F. Perez, Pérez-Molina, L., Pernas, C., Perry, J., Pershey, D., Pessina, G., Petrillo, G., Petta, C., Petti, R., Pfaff, M., Pia, V., Pickering, L., Pietropaolo, F., Pimentel, V. L., Pinaroli, G., Pincha, S., Pinchault, J., Pitts, K., Plows, K., Pollack, C., Pollman, T., Pompa, F., Pons, X., Poonthottathil, N., Popov, V., Poppi, F., Porter, J., Paixão, L. G. Porto, Potekhin, M., Potenza, R., Pozzato, M., Prakash, T., Pratt, C., Prest, M., Psihas, F., Pugnere, D., Qian, X., Queen, J., Raaf, J. L., Radeka, V., Rademacker, J., Radics, B., Raffaelli, F., Rafique, A., Raguzin, E., Rahaman, U., Rai, M., Rajagopalan, S., Rajaoalisoa, M., Rakhno, I., Rakotondravohitra, L., Ralte, L., Delgado, M. A. Ramirez, Ramson, B., Rappoldi, A., Raselli, G., Ratoff, P., Ray, R., Razafinime, H., Razakamiandra, R. F., Rea, E. M., Real, J. S., Rebel, B., Rechenmacher, R., Reichenbacher, J., Reitzner, S. D., Sfar, H. Rejeb, Renner, E., Renshaw, A., Rescia, S., Resnati, F., Restrepo, Diego, Reynolds, C., Ribas, M., Riboldi, S., Riccio, C., Riccobene, G., Ricol, J. S., Rigan, M., Rincón, E. V., Ritchie-Yates, A., Ritter, S., Rivera, D., Rivera, R., Robert, A., Rocha, J. L. Rocabado, Rochester, L., Roda, M., Rodrigues, P., Alonso, M. J. Rodriguez, Rondon, J. Rodriguez, Rosauro-Alcaraz, S., Rosier, P., Ross, D., Rossella, M., Rossi, M., Ross-Lonergan, M., Roy, N., Roy, P., Rubbia, C., Ruggeri, A., Ferreira, G. Ruiz, Russell, B., Ruterbories, D., Rybnikov, A., Sacerdoti, S., Saha, S., Sahoo, S. K., Sahu, N., Sala, P., Samios, N., Samoylov, O., Sanchez, M. C., Bravo, A. Sánchez, Sánchez-Castillo, A., Sanchez-Lucas, P., Sandberg, V., Sanders, D. A., Sanfilippo, S., Sankey, D., Santoro, D., Saoulidou, N., Sapienza, P., Sarasty, C., Sarcevic, I., Sarra, I., Savage, G., Savinov, V., Scanavini, G., Scaramelli, A., Scarff, A., Schefke, T., Schellman, H., Schifano, S., Schlabach, P., Schmitz, D., Schneider, A. W., Scholberg, K., Schukraft, A., Schuld, B., Segade, A., Segreto, E., Selyunin, A., Senadheera, D., Senise, C. R., Sensenig, J., Shaevitz, M. H., Shanahan, P., Sharma, P., Kumar, R., Poudel, S. Sharma, Shaw, K., Shaw, T., Shchablo, K., Shen, J., Shepherd-Themistocleous, C., Sheshukov, A., Shi, J., Shi, W., Shin, S., Shivakoti, S., Shoemaker, I., Shooltz, D., Shrock, R., Siddi, B., Siden, M., Silber, J., Simard, L., Sinclair, J., Sinev, G., Singh, Jaydip, Singh, J., Singh, L., Singh, P., Singh, V., Chauhan, S. Singh, Sipos, R., Sironneau, C., Sirri, G., Siyeon, K., Skarpaas, K., Smedley, J., Smith, E., Smith, J., Smith, P., Smolik, J., Smy, M., Snape, M., Snider, E. L., Snopok, P., Snowden-Ifft, D., Nunes, M. Soares, Sobel, H., Soderberg, M., Sokolov, S., Salinas, C. J. Solano, Söldner-Rembold, S., Solomey, N., Solovov, V., Sondheim, W. E., Sorel, M., Sotnikov, A., Soto-Oton, J., Sousa, A., Soustruznik, K., Spinella, F., Spitz, J., Spooner, N. J. C., Spurgeon, K., Stalder, D., Stancari, M., Stanco, L., Steenis, J., Stein, R., Steiner, H. M., Lisbôa, A. F. Steklain, Stepanova, A., Stewart, J., Stillwell, B., Stock, J., Stocker, F., Stokes, T., Strait, M., Strauss, T., Strigari, L., Stuart, A., Suarez, J. G., Subash, J., Surdo, A., Suter, L., Sutera, C. M., Sutton, K., Suvorov, Y., Svoboda, R., Swain, S. K., Szczerbinska, B., Szelc, A. M., Sztuc, A., Taffara, A., Talukdar, N., Tamara, J., Tanaka, H. A., Tang, S., Taniuchi, N., Casanova, A. M. Tapia, Oregui, B. Tapia, Tapper, A., Tariq, S., Tarpara, E., Tatar, E., Tayloe, R., Tedeschi, D., Teklu, A. M., Vidal, J. Tena, Tennessen, P., Tenti, M., Terao, K., Terranova, F., Testera, G., Thakore, T., Thea, A., Thomas, S., Thompson, A., Thorn, C., Timm, S. C., Tiras, E., Tishchenko, V., Tiwari, S., Todorović, N., Tomassetti, L., Tonazzo, A., Torbunov, D., Torti, M., Tortola, M., Tortorici, F., Tosi, N., Totani, D., Toups, M., Touramanis, C., Tran, D., Travaglini, R., Trevor, J., Triller, E., Trilov, S., Truchon, J., Truncali, D., Trzaska, W. H., Tsai, Y., Tsai, Y. -T., Tsamalaidze, Z., Tsang, K. V., Tsverava, N., Tu, S. Z., Tufanli, S., Tunnell, C., Turnberg, S., Turner, J., Tuzi, M., Tyler, J., Tyley, E., Tzanov, M., Uchida, M. A., González, J. Ureña, Urheim, J., Usher, T., Utaegbulam, H., Uzunyan, S., Vagins, M. R., Vahle, P., Valder, S., Valdiviesso, G. A., Valencia, E., Valentim, R., Vallari, Z., Vallazza, E., Valle, J. W. F., Van Berg, R., Van de Water, R. G., Forero, D. V., Vannozzi, A., Van Nuland-Troost, M., Varanini, F., Oliva, D. Vargas, Vasina, S., Vaughan, N., Vaziri, K., Vázquez-Ramos, A., Vega, J., Ventura, S., Verdugo, A., Vergani, S., Verzocchi, M., Vetter, K., Vicenzi, M., de Souza, H. Vieira, Vignoli, C., Vilela, C., Villa, E., Viola, S., Viren, B., Vizarreta, R., Hernandez, A. P. Vizcaya, Vuong, Q., Waldron, A. V., Wallbank, M., Walsh, J., Walton, T., Wang, H., Wang, J., Wang, L., Wang, M. H. L. S., Wang, X., Wang, Y., Warburton, K., Warner, D., Warsame, L., Wascko, M. O., Waters, D., Watson, A., Wawrowska, K., Weber, A., Weber, C. M., Weber, M., Wei, H., Weinstein, A., Westerdale, S., Wetstein, M., Whalen, K., White, A., Whitehead, L. H., Whittington, D., Wilhlemi, J., Wilking, M. J., Wilkinson, A., Wilkinson, C., Wilson, F., Wilson, R. J., Winter, P., Wisniewski, W., Wolcott, J., Wolfs, J., Wongjirad, T., Wood, A., Wood, K., Worcester, E., Worcester, M., Wospakrik, M., Wresilo, K., Wret, C., Wu, S., Wu, W., Wurm, M., Wyenberg, J., Xiao, Y., Xiotidis, I., Yaeggy, B., Yahlali, N., Yandel, E., Yang, J., Yang, K., Yang, T., Yankelevich, A., Yershov, N., Yonehara, K., Young, T., Yu, B., Yu, H., Yu, J., Yu, Y., Yuan, W., Zaki, R., Zalesak, J., Zambelli, L., Zamorano, B., Zani, A., Zapata, O., Zazueta, L., Zeller, G. P., Zennamo, J., Zeug, K., Zhang, C., Zhang, S., Zhao, M., Zhivun, E., Zimmerman, E. D., Zucchelli, S., Zuklin, J., Zutshi, V., and Zwaska, R.
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Physics - Instrumentation and Detectors ,High Energy Physics - Experiment - Abstract
This paper introduces the hypothetical track-length fitting algorithm, a novel method for measuring the kinetic energies of ionizing particles in liquid argon time projection chambers (LArTPCs). The algorithm finds the most probable offset in track length for a track-like object by comparing the measured ionization density as a function of position with a theoretical prediction of the energy loss as a function of the energy, including models of electron recombination and detector response. The algorithm can be used to measure the energies of particles that interact before they stop, such as charged pions that are absorbed by argon nuclei. The algorithm's energy measurement resolutions and fractional biases are presented as functions of particle kinetic energy and number of track hits using samples of stopping secondary charged pions in data collected by the ProtoDUNE-SP detector, and also in a detailed simulation. Additional studies describe impact of the dE/dx model on energy measurement performance. The method described in this paper to characterize the energy measurement performance can be repeated in any LArTPC experiment using stopping secondary charged pions.
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- 2024
30. Molecular Machinery of the Triad Holin, Endolysin, and Spanin: Key Players Orchestrating Bacteriophage-Induced Cell Lysis and their Therapeutic Applications.
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Samir, Safia, primary
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- 2024
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31. Spatial and temporal control of lysis by the lambda holin
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Cahill, Jesse, primary, Holt, Ashley, additional, Theodore, Matthew, additional, Moreland, Russell, additional, O'Leary, Chandler, additional, Martin, Cody, additional, Bettridge, Kelsey, additional, Xiao, Jie, additional, and Young, Ry, additional
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- 2023
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32. A holin/peptidoglycan hydrolase-dependent protein secretion system
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Palmer, Tracy, Finney, Alexander, Saha, Chayan Kumar, Atkinson, Gemma C., Sargent, Frank, Palmer, Tracy, Finney, Alexander, Saha, Chayan Kumar, Atkinson, Gemma C., and Sargent, Frank
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Gram-negative bacteria have evolved numerous pathways to secrete proteins across their complex cell envelopes. Here, we describe a protein secretion system which uses a holin membrane protein in tandem with a cell wall editing enzyme to mediate the secretion of substrate proteins from the periplasm to the cell exterior. The identity of the cell wall editing enzymes employed was found to vary across biological systems. For instance, the chitinase secretion pathway of Serratia marcescens uses an endopeptidase to facilitate secretion, whereas the secretion of Typhoid toxin in Salmonella enterica serovar Typhi relies on a muramidase. Various families of holins are also predicted to be involved. Genomic analysis indicates that this pathway is conserved and implicated in the secretion of hydrolytic enzymes and toxins for a range of bacteria. The pairing of holins from different families with various types of peptidoglycan hydrolases suggests that this secretion pathway evolved multiple times. We suggest that the complementary bodies of evidence presented is sufficient to propose that the pathway be named the Type 10 Secretion System (TXSS). Potential mechanisms for secretion across the outer membrane are discussed., Special Issue: Protein Secretion and Transport
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- 2021
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33. Bioinformatic characterization of endolysins and holin-like membrane proteins in the lysis cassette of phages that infect Gordonia rubripertincta.
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Richard S Pollenz, Jackson Bland, and Welkin H Pope
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Medicine ,Science - Abstract
Holins are bacteriophage-encoded transmembrane proteins that function to control the timing of bacterial lysis event, assist with the destabilization of the membrane proton motive force and in some models, generate large "pores" in the cell membrane to allow the exit of the phage-encoded endolysin so they can access the peptidoglycan components of the cell wall. The lysis mechanism has been rigorously evaluated through biochemical and genetic studies in very few phages, and the results indicate that phages utilize endolysins, holins and accessory proteins to the outer membrane to achieve cell lysis through several distinct operational models. This observation suggests the possibility that phages may evolve novel variations of how the lysis proteins functionally interact in an effort to improve fitness or evade host defenses. To begin to address this hypothesis, the current study utilized a comprehensive bioinformatic approach to systematically identify the proteins encoded by the genes within the lysis cassettes in 16 genetically diverse phages that infect the Gram-positive Gordonia rubripertincta NRLL B-16540 strain. The results show that there is a high level of diversity of the various lysis genes and 16 different genome organizations of the putative lysis cassette, many which have never been described. Thirty-four different genes encoding holin-like proteins were identified as well as a potential holin-major capsid fusion protein. The holin-like proteins contained between 1-4 transmembrane helices, were not shared to a high degree amongst the different phages and are present in the lysis cassette in a wide range of combinations of up to 4 genes in which none are duplicated. Detailed evaluation of the transmembrane domains and predicted membrane topologies of the holin-like proteins show that many have novel structures that have not been previously characterized. These results provide compelling support that there are novel operational lysis models yet to be discovered.
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- 2022
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34. Regulation and Functionality of a Holin/Endolysin Pair Involved in Killing of Galleria mellonella and Caenorhabditis elegans by Yersinia enterocolitica.
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Sänger, Philipp-Albert, Knüpfer, Mandy, Kegel, Marcel, Spanier, Britta, Liebler-Tenorio, Elisabeth M., and Fuchs, Thilo M.
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YERSINIA enterocolitica , *GREATER wax moth , *BACILLUS thuringiensis , *CAENORHABDITIS elegans , *BACTERIAL toxins , *LIFE cycles (Biology) , *INSECT larvae , *QUORUM sensing - Abstract
The insecticidal toxin complex (Tc) proteins are produced by several insect-associated bacteria, including Yersinia enterocolitica strain W22703, which oscillates between two distinct pathogenicity phases in invertebrates and humans. The mechanism by which this high-molecular-weight toxin is released into the extracellular surrounding, however, has not been deciphered. In this study, we investigated the regulation and functionality of a phage-related holin/endolysin (HE) cassette located within the insecticidal pathogenicity island Tc-PAIYe of W22703. Using the Galleria mellonella infection model and luciferase reporter fusions, we revealed that quorum sensing contributes to the insecticidal activity of W22703 upon influencing the transcription of tcaR2, which encodes an activator of the tc and HE genes. In contrast, a lack of the Yersinia modulator, YmoA, stimulated HE gene transcription, and mutant W22703 ΔymoA exhibited a stronger toxicity toward insect larvae than did W22703. A luciferase reporter fusion demonstrated transcriptional activation of the HE cassette in vivo, and a significantly larger extracellular amount of subunit TcaA was found in W22703 ΔymoA relative to its ΔHE mutant. Using competitive growth assays, we demonstrated that at least in vitro, the TcaA release upon HE activity is not mediated by cell lysis of a significant part of the population. Oral infection of Caenorhabditis elegans with a HE deletion mutant attenuated the nematocidal activity of the wild type, similar to the case with a mutant lacking a Tc subunit. We conclude that the dual holin/endolysin cassette of yersiniae is a novel example of a phage-related function adapted for the release of a bacterial toxin. IMPORTANCE Members of the genus Yersinia cause gastroenteritis in humans but also exhibit toxicity toward invertebrates. A virulence factor required for this environmental life cycle stage is the multisubunit toxin complex (Tc), which is distinct from the insecticidal toxin of Bacillus thuringiensis and has the potential to be used in pest control. The mechanism by which this high-molecular-weight Tc is secreted from bacterial cells has not been uncovered. Here, we show that a highly conserved phage-related holin/endolysin pair, which is encoded by the genes holY and elyY located between the Tc subunit genes, is essential for the insecticidal activity of Y. enterocolitica and that its activation increases the amount of Tc subunits in the supernatant. Thus, the dual holY-elyY cassette of Y. enterocolitica constitutes a new example for a type 10 secretion system to release bacterial toxins. [ABSTRACT FROM AUTHOR]
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- 2023
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35. Načrtovanje, sinteza in vrednotenje novih zaviralcev holin-esteraz
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Košak, Urban and Gobec, Stanislav
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vrednotenje ,načrtovanje ,sinteza ,zdravljenje ,udc:615.21:616.894(043.3) ,Alzheimerjeva bolezen ,nevrodegenerativne bolezni ,zaviralci holin-esteraz ,disertacije - Abstract
Alzheimerjeva bolezen je kronična progresivna nevrodegenerativna bolezen možganov. Vzroki za nastanek te bolezni še niso znani, je pa znano, da kopičenje amiloidni proteina β, proteina tau in oksidativni stres v možganih povzročijo odmiranje nevronov in propadanje sinaps. Ta nevrodegeneracija je najizrazitejša v holinergičnem živčno-prenašalnem sistemu. Posledica tega je zmanjšana koncentracija živčnega prenašalca acetilholina v možganih, kar povzroči motnje spomina, ki so značilne za bolnike z Alzheimerjevo boleznijo. Trenutno zdravljenje ali preprečevanje te bolezni ni mogoče in bolnikom so na voljo le štiri učinkovine za lajšanje simptomov. Holin-esterazi acetilholin-esteraza in butirilholin-esteraza prekineta holinergični živčni prenos v možganih tako, da katalizirata hidrolizo acetilholina. V možganih zdravih odraslih je acetilholin-esteraza odgovorna za 80%, butirilholin-esteraza pa za 20% holin-esterazne encimske aktivnosti. Z napredovanjem bolezni se encimska aktivnost acetilholin-esteraze zmanjšuje, butirilholin-esteraze pa povečuje. Tri od štirih učinkovin za lajšanje simptomov Alzheimerjeve bolezni so zaviralci holin-esteraz: selektivna zaviralca acetilholin-esteraze donepezil in galantamin ter zaviralec acetilholin-esteraze in butirilholin-esteraze rivastigmin. Te učinkovine imajo, zaradi zaviranja acetilholin-esteraze, številne slabosti (neželeni učinki zaradi zaviranja acetilholin-esteraze v perifernem živčnem sistemu in s tem povezan omejen odmerek ter neučinkovitost v poznih stadijih bolezni), katerim se da izogniti s selektivnim zaviranjem butirilholin-esteraze. Načrtovali, sintetizirali in ovrednotili smo obsežno serijo novih selektivnih reverzibilnih zaviralcev butirilholin-esteraze: sulfonamidne in N-propargilpiperidinske derivate spojine zadetka 1 (IC50 = 21,3 nM) in določili odnos med njihovo strukturo in delovanjem. Za sintezo ključih intermediatov v sintezni poti do načrtovanih zaviralcev smo razvili splošni in enostavni sintezni postopek. Sulfonamidni derivat 2 (IC50 = 4,9 nM) je obetavna spojini za nadaljnji predklinični razvoj. Spojina ni citotoksična in ščiti živčne celice pred strupenimi amiloidnega proteina β. Zavira butirilholin-esterazo v rezinah podganjih možganov in prehaja v možgane podgan po intraperitonealni aplikaciji. Dokazali smo, da spojina 2 izboljša spomin, kognitivne funkcije in učne sposobnosti miši v bolezenskem modelu zmanjšane holinergične aktivnosti pri Alzheimerjevi bolezni. V možganih bolnikov je povišana encimska aktivnost monoaminske oksidaze B. Produkti, ki nastanejo pri reakciji, ki jo katalizira ta encim, prispevajo k oksidativnemu stresu in nevrodegeneraciji pri Alzheimerjevi bolezni. Trije N-propargilpiperidnski derivati spojine zadetka 1 poleg butirilholin-esteraze zavirajo tudi monoaminsko oksidazo B. Zaviralec obeh encimov z nevroprotektivnim delovanjem (N-propargilpiperidin 6) je spojina vodnica za načrtovanje novih spojin z delovanjem na več tarč. V doktorski disertaciji predstavljamo, da smo s sistematičnimi spremembami strukture spojine zadetka 1 prišli do (i) obetavne spojine za nadaljni predklinični razvoj, (ii) štirih kristalnih struktur kompleksov butirilholin-esteraz z zaviralci, (iii) ortogonalno zaščitenih intermediatov za sintezo novih zaviralcev in (iv) spojine vodnice kot izhodišča za načrtovanje novih spojin z delovanjem na več tarč. Alzheimer's disease is a chronic progressive neurodegenerative brain disorder. The etiology of this disease is not entirely understood, although it is known that accumulation of amyloid β peptide, protein tau and oxidative stress in the brain cause neuronal death and synaptic loss. This neurodegeneration is most severe in the cholinergic neurotransmitter system and results in a decrease in the levels of the neurotransmitter acetylcholine, which in turn produces memory deficits, characteristic for patients with Alzheimer's disease. Currently, there are no means to cure or prevent Alzheimer's disease, and only four drugs are available to patients for alleviating its symptoms. Cholinesterases acetylcholinesterase and butyrycholinesterase terminate cholinergic neurotransmission in the brain by catalyzing the hydrolysis of acetylcholine. In the healthy brain, acetylcholinesterase accounts for 80% and butyrycholinesterase accounts for 20% of the cholinesterase enzymatic activity. As the disease progresses, enzymatic activity of acetylcholinesterase is reduced, while that of butyrycholinesterase increases. Three out of the four approved drugs for alleviating symptoms of patients with AD are cholinesterase inhibitors: the selective acetycholinesterase inhibitors donepezil and galantamine, and the pseudo-irreversible acetylcholinesterase and butyrycholinesterase inhibitor rivastigmine. These drugs have numerous limitations due to inhibition of acetycholinesterase (adverse side effects due to acetylcholinesterase inhibition in the peripheral nervous system, limited dosing and limited clinical efficacy in advanced stages of the disease) which can be overcome by selectively inhibiting butyrylcholinesterase. We have designed, synthesized and evaluated a comprehensive series of new selective reversible butyrycholinesterase inhibitors: sulfonamide and N-propargypiperidine derivatives of hit compound 1 (IC50 = 21.3 nM) and determined their structure–activity relationships. For preparing key intermediates in the synthesis of designed compounds, we developed a general and simple synthetic procedure. Sulfonamide derivative 2 (IC50 = 4.9 nM) is promising candidate for further preclinical development. This compound is noncytotoxic and protects neuronal cells from toxic amyloid β peptide species. Its inhibits butyrycholinesterase in rat brain slices and partitions into the brains of rats after intraperitoneal injection. Compound 2 and improves memory, cognitive functions, and learning abilities of mice in a disease model of the cholinergic hypofunction in Alzheimer's disease. In the brains of patients with Alzheimer's disease the enzymatic activity of monoamine oxidase B is increased and products formed in the reaction catalyzed by this enzyme contribute to the neurodegeneration. We developed three N-propargypiperidines derivatives of hit compound 1 that inhibit both butyrycholinesterase and monoamine oxidase B. N-propargylpiperidine 6 also has neuroprotective activity and therefore represents a lead compound for design of multitarget-directed ligands against Alzheimer’s disease. In this thesis, we describe the use of structural modifications of hit compound 1 to obtain (i) a promising candidate for further preclinical development, (ii) four crystal structures of complexes of butyrycholinesterase with its inhibitors, (iii) orthogonally protected intermediates for synthesis of new cholinesterase inhibitors, and (iv) lead compounds for design of new multitarget-directed ligands.
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- 2023
36. DUNE Phase II: Scientific Opportunities, Detector Concepts, Technological Solutions
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DUNE Collaboration, Abud, A. Abed, Abi, B., Acciarri, R., Acero, M. A., Adames, M. R., Adamov, G., Adamowski, M., Adams, D., Adinolfi, M., Adriano, C., Aduszkiewicz, A., Aguilar, J., Akbar, F., Allison, K., Monsalve, S. Alonso, Alrashed, M., Alton, A., Alvarez, R., Alves, T., Amar, H., Amedo, P., Anderson, J., Andreopoulos, C., Andreotti, M., Andrews, M. P., Andrianala, F., Andringa, S., Anfimov, N., Ankowski, A., Antic, D., Antoniassi, M., Antonova, M., Antoshkin, A., Aranda-Fernandez, A., Arellano, L., Diaz, E. Arrieta, Arroyave, M. A., Asaadi, J., Ashkenazi, A., Asner, D. M., Asquith, L., Atkin, E., Auguste, D., Aurisano, A., Aushev, V., Autiero, D., Azam, M. B., Azfar, F., Back, A., Back, H., Back, J. J., Bagaturia, I., Bagby, L., Balashov, N., Balasubramanian, S., Baldi, P., Baldini, W., Baldonedo, J., Baller, B., Bambah, B., Banerjee, R., Barao, F., Barbu, D., Barenboim, G., Barham~Alzás, P., Barker, G. J., Barkhouse, W., Barr, G., Monarca, J. Barranco, Barros, A., Barros, N., Barrow, D., Barrow, J. L., Basharina-Freshville, A., Bashyal, A., Basque, V., Batchelor, C., Bathe-Peters, L., Battat, J. B. R., Battisti, F., Bay, F., Bazetto, M. C. Q., Alba, J. L. L. Bazo, Beacom, J. F., Bechetoille, E., Behera, B., Belchior, E., Bell, G., Bellantoni, L., Bellettini, G., Bellini, V., Beltramello, O., Benekos, N., Montiel, C. Benitez, Benjamin, D., Neves, F. Bento, Berger, J., Berkman, S., Bernal, J., Bernardini, P., Bersani, A., Bertolucci, S., Betancourt, M., Rodríguez, A. Betancur, Bevan, A., Bezawada, Y., Bezerra, A. T., Bezerra, T. J., Bhat, A., Bhatnagar, V., Bhatt, J., Bhattacharjee, M., Bhattacharya, M., Bhuller, S., Bhuyan, B., Biagi, S., Bian, J., Biery, K., Bilki, B., Bishai, M., Bitadze, A., Blake, A., Blaszczyk, F. D., Blazey, G. C., Blucher, E., Bodek, A., Bogenschuetz, J., Boissevain, J., Bolognesi, S., Bolton, T., Bomben, L., Bonesini, M., Bonilla-Diaz, C., Bonini, F., Booth, A., Boran, F., Bordoni, S., Merlo, R. Borges, Borkum, A., Bostan, N., Bouet, R., Boza, J., Bracinik, J., Brahma, B., Brailsford, D., Bramati, F., Branca, A., Brandt, A., Bremer, J., Brew, C., Brice, S. J., Brio, V., Brizzolari, C., Bromberg, C., Brooke, J., Bross, A., Brunetti, G., Brunetti, M., Buchanan, N., Budd, H., Buergi, J., Bundock, A., Burgardt, D., Butchart, S., V., G. Caceres, Cagnoli, I., Cai, T., Calabrese, R., Calcutt, J., Calivers, L., Calvo, E., Caminata, A., Camino, A. F., Campanelli, W., Campani, A., Benitez, A. Campos, Canci, N., Capó, J., Caracas, I., Caratelli, D., Carber, D., Carceller, J. M., Carini, G., Carlus, B., Carneiro, M. F., Carniti, P., Terrazas, I. Caro, Carranza, H., Carrara, N., Carroll, L., Carroll, T., Carter, A., Casarejos, E., Casazza, D., Forero, J. F. Castaño, Castaño, F. A., Castillo, A., Castromonte, C., Catano-Mur, E., Cattadori, C., Cavalier, F., Cavanna, F., Centro, S., Cerati, G., Cerna, C., Cervelli, A., Villanueva, A. Cervera, Chakraborty, K., Chakraborty, S., Chalifour, M., Chappell, A., Charitonidis, N., Chatterjee, A., Chen, H., Chen, M., Chen, W. C., Chen, Y., Chen-Wishart, Z., Cherdack, D., Chi, C., Chiapponi, F., Chirco, R., Chitirasreemadam, N., Cho, K., Choate, S., Chokheli, D., Chong, P. S., Chowdhury, B., Christian, D., Chukanov, A., Chung, M., Church, E., Cicala, M. F., Cicerchia, M., Cicero, V., Ciolini, R., Clarke, P., Cline, G., Coan, T. E., Cocco, A. G., Coelho, J. A. B., Cohen, A., Collazo, J., Collot, J., Conley, E., Conrad, J. M., Convery, M., Copello, S., Cortez, A. F. V., Cova, P., Cox, C., Cremaldi, L., Cremonesi, L., Crespo-Anadón, J. I., Crisler, M., Cristaldo, E., Crnkovic, J., Crone, G., Cross, R., Cudd, A., Cuesta, C., Cui, Y., Curciarello, F., Cussans, D., Dai, J., Dalager, O., Dallavalle, R., Dallaway, W., D'Amico, R., da Motta, H., Dar, Z. A., Darby, R., Peres, L. Da Silva, David, Q., Davies, G. S., Davini, S., Dawson, J., De Aguiar, R., De Almeida, P., Debbins, P., De Bonis, I., Decowski, M. P., de Gouvêa, A., De Holanda, P. C., Astiz, I. L. De Icaza, De Jong, P., Sanchez, P. Del Amo, De la Torre, A., De Lauretis, G., Delbart, A., Delepine, D., Delgado, M., Dell'Acqua, A., Monache, G. Delle, Delmonte, N., De Lurgio, P., Demario, R., De Matteis, G., Neto, J. R. T. de Mello, DeMuth, D. M., Dennis, S., Densham, C., Denton, P., Deptuch, G. W., De Roeck, A., De Romeri, V., Detje, J. P., Devine, J., Dharmapalan, R., Dias, M., Diaz, A., Díaz, J. S., Díaz, F., Di Capua, F., Di Domenico, A., Di Domizio, S., Di Falco, S., Di Giulio, L., Ding, P., Di Noto, L., Diociaiuti, E., Distefano, C., Diurba, R., Diwan, M., Djurcic, Z., Doering, D., Dolan, S., Dolek, F., Dolinski, M. J., Domenici, D., Domine, L., Donati, S., Donon, Y., Doran, S., Douglas, D., Doyle, T. A., Dragone, A., Drielsma, F., Duarte, L., Duchesneau, D., Duffy, K., Dugas, K., Dunne, P., Dutta, B., Duyang, H., Dwyer, D. A., Dyshkant, A. S., Dytman, S., Eads, M., Earle, A., Edayath, S., Edmunds, D., Eisch, J., Englezos, P., Ereditato, A., Erjavec, T., Escobar, C. O., Evans, J. J., Ewart, E., Ezeribe, A. C., Fahey, K., Fajt, L., Falcone, A., Fani', M., Farnese, C., Farrell, S., Farzan, Y., Fedoseev, D., Felix, J., Feng, Y., Fernandez-Martinez, E., Fernández-Posada, D., Ferry, G., Fialova, E., Fields, L., Filip, P., Filkins, A., Filthaut, F., Fine, R., Fiorillo, G., Fiorini, M., Fogarty, S., Foreman, W., Fowler, J., Franc, J., Francis, K., Franco, D., Franklin, J., Freeman, J., Fried, J., Friedland, A., Fuess, S., Furic, I. K., Furman, K., Furmanski, A. P., Gaba, R., Gabrielli, A., M~Gago, A., Galizzi, F., Gallagher, H., Gallice, N., Galymov, V., Gamberini, E., Gamble, T., Ganacim, F., Gandhi, R., Ganguly, S., Gao, F., Gao, S., Garcia-Gamez, D., García-Peris, M. Á., Gardim, F., Gardiner, S., Gastler, D., Gauch, A., Gauvreau, J., Gauzzi, P., Gazzana, S., Ge, G., Geffroy, N., Gelli, B., Gent, S., Gerlach, L., Ghorbani-Moghaddam, Z., Giammaria, T., Gibin, D., Gil-Botella, I., Gilligan, S., Gioiosa, A., Giovannella, S., Girerd, C., Giri, A. K., Giugliano, C., Giusti, V., Gnani, D., Gogota, O., Gollapinni, S., Gollwitzer, K., Gomes, R. A., Bermeo, L. V. Gomez, Fajardo, L. S. Gomez, Gonnella, F., Gonzalez-Diaz, D., Gonzalez-Lopez, M., Goodman, M. C., Goswami, S., Gotti, C., Goudeau, J., Goudzovski, E., Grace, C., Gramellini, E., Gran, R., Granados, E., Granger, P., Grant, C., Gratieri, D. R., Grauso, G., Green, P., Greenberg, S., Greer, J., Griffith, W. C., Groetschla, F. T., Grzelak, K., Gu, L., Gu, W., Guarino, V., Guarise, M., Guenette, R., Guerzoni, M., Guffanti, D., Guglielmi, A., Guo, B., Guo, F. Y., Gupta, A., Gupta, V., Gurung, G., Gutierrez, D., Guzowski, P., Guzzo, M. M., Gwon, S., Habig, A., Hadavand, H., Haegel, L., Haenni, R., Hagaman, L., Hahn, A., Haiston, J., Hakenmüller, J., Hamernik, T., Hamilton, P., Hancock, J., Happacher, F., Harris, D. A., Hart, A., Hartnell, J., Hartnett, T., Harton, J., Hasegawa, T., Hasnip, C. M., Hatcher, R., Hayrapetyan, K., Hays, J., Hazen, E., He, M., Heavey, A., Heeger, K. M., Heise, J., Hellmuth, P., Henry, S., Hernández-García, J., Herner, K., Hewes, V., Higuera, A., Hilgenberg, C., Hillier, S. J., Himmel, A., Hinkle, E., Hirsch, L. R., Ho, J., Hoff, J., Holin, A., Holvey, T., Hoppe, E., Horiuchi, S., Horton-Smith, G. A., Houdy, T., Howard, B., Howell, R., Hristova, I., Hronek, M. S., Huang, J., Huang, R. G., Hulcher, Z., Ibrahim, M., Iles, G., Ilic, N., Iliescu, A. M., Illingworth, R., Ingratta, G., Ioannisian, A., Irwin, B., Isenhower, L., Oliveira, M. Ismerio, Itay, R., Jackson, C. M., Jain, V., James, E., Jang, W., Jargowsky, B., Jena, D., Jentz, I., Ji, X., Jiang, C., Jiang, J., Jiang, L., Jipa, A., Jo, J. H., Joaquim, F. R., Johnson, W., Jollet, C., Jones, B., Jones, R., Jovancevic, N., Judah, M., Jung, C. K., Junk, T., Jwa, Y., Kabirnezhad, M., Kaboth, A. C., Kadenko, I., Kakorin, I., Kalitkina, A., Kalra, D., Kandemir, M., Kaplan, D. M., Karagiorgi, G., Karaman, G., Karcher, A., Karyotakis, Y., Kasai, S., Kasetti, S. P., Kashur, L., Katsioulas, I., Kauther, A., Kazaryan, N., Ke, L., Kearns, E., Keener, P. T., Kelly, K. J., Kemp, E., Kemularia, O., Kermaidic, Y., Ketchum, W., Kettell, S. H., Khabibullin, M., Khan, N., Khvedelidze, A., Kim, D., Kim, J., Kim, M. J., King, B., Kirby, B., Kirby, M., Kish, A., Klein, J., Kleykamp, J., Klustova, A., Kobilarcik, T., Koch, L., Koehler, K., Koerner, L. W., Koh, D. H., Kolupaeva, L., Korablev, D., Kordosky, M., Kosc, T., Kose, U., Kostelecký, V. A., Kothekar, K., Kotler, I., Kovalcuk, M., Kozhukalov, V., Krah, W., Kralik, R., Kramer, M., Kreczko, L., Krennrich, F., Kreslo, I., Kroupova, T., Kubota, S., Kubu, M., Kudenko, Y., Kudryavtsev, V. A., Kufatty, G., Kuhlmann, S., Kulagin, S., Kumar, J., Kumar, P., Kumaran, S., Kunzmann, J., Kuravi, R., Kurita, N., Kuruppu, C., Kus, V., Kutter, T., Kuźniak, M., Kvasnicka, J., Labree, T., Lackey, T., Lalău, I., Lambert, A., Land, B. J., Lane, C. E., Lane, N., Lang, K., Langford, T., Langstaff, M., Lanni, F., Lantwin, O., Larkin, J., Lasorak, P., Last, D., Laudrain, A., Laundrie, A., Laurenti, G., Lavaut, E., Laycock, P., Lazanu, I., LaZur, R., Lazzaroni, M., Le, T., Leardini, S., Learned, J., LeCompte, T., Legin, V., Miotto, G. Lehmann, Lehnert, R., de Oliveira, M. A. Leigui, Leitner, M., Silverio, D. Leon, Lepin, L. M., -Y~Li, J., Li, S. W., Li, Y., Liao, H., Lin, C. S., Lindebaum, D., Linden, S., Lineros, R. A., Lister, A., Littlejohn, B. R., Liu, H., Liu, J., Liu, Y., Lockwitz, S., Lokajicek, M., Lomidze, I., Long, K., Lopes, T. V., Lopez, J., de Rego, I. López, López-March, N., Lord, T., LoSecco, J. M., Louis, W. C., Sanchez, A. Lozano, Lu, X. -G., Luk, K. B., Lunday, B., Luo, X., Luppi, E., MacFarlane, D., Machado, A. A., Machado, P., Macias, C. T., Macier, J. R., MacMahon, M., Maddalena, A., Madera, A., Madigan, P., Magill, S., Magueur, C., Mahn, K., Maio, A., Major, A., Majumdar, K., Mameli, S., Man, M., Mandujano, R. C., Maneira, J., Manly, S., Mann, A., Manolopoulos, K., Plata, M. Manrique, Corchado, S. Manthey, Manyam, V. N., Marchan, M., Marchionni, A., Marciano, W., Marfatia, D., Mariani, C., Maricic, J., Marinho, F., Marino, A. D., Markiewicz, T., Marques, F. Das Chagas, Marquet, C., Marshak, M., Marshall, C. M., Marshall, J., Martina, L., Martín-Albo, J., Martinez, N., Caicedo, D. A. Martinez, López, F. Martínez, Miravé, P. Martínez, Martynenko, S., Mascagna, V., Massari, C., Mastbaum, A., Matichard, F., Matsuno, S., Matteucci, G., Matthews, J., Mauger, C., Mauri, N., Mavrokoridis, K., Mawby, I., Mazza, R., McAskill, T., McConkey, N., McFarland, K. S., McGrew, C., McNab, A., Meazza, L., Meddage, V. C. N., Mefodiev, A., Mehta, B., Mehta, P., Melas, P., Mena, O., Mendez, H., Mendez, P., Méndez, D. P., Menegolli, A., Meng, G., Mercuri, A. C. E. A., Meregaglia, A., Messier, M. D., Metallo, S., Metcalf, W., Mewes, M., Meyer, H., Miao, T., Micallef, J., Miccoli, A., Michna, G., Milincic, R., Miller, F., Miller, G., Miller, W., Mineev, O., Minotti, A., Miralles, L., Miranda, O. G., Mironov, C., Miryala, S., Miscetti, S., Mishra, C. S., Mishra, P., Mishra, S. R., Mislivec, A., Mitchell, M., Mladenov, D., Mocioiu, I., Mogan, A., Moggi, N., Mohanta, R., Mohayai, T. A., Mokhov, N., Molina, J., Bueno, L. Molina, Montagna, E., Montanari, A., Montanari, C., Montanari, D., Montanino, D., Zetina, L. M. Montaño, Mooney, M., Moor, A. F., Moore, Z., Moreno, D., Moreno-Palacios, O., Morescalchi, L., Moretti, D., Moretti, R., Morris, C., Mossey, C., Moura, C. A., Mouster, G., Mu, W., Mualem, L., Mueller, J., Muether, M., Muheim, F., Muir, A., Mulhearn, M., Munford, D., Munteanu, L. J., Muramatsu, H., Muraz, J., Murphy, M., Murphy, T., Muse, J., Mytilinaki, A., Nachtman, J., Nagai, Y., Nagu, S., Nandakumar, R., Naples, D., Narita, S., Navrer-Agasson, A., Nayak, N., Nebot-Guinot, M., Nehm, A., Nelson, J. K., Neogi, O., Nesbit, J., Nessi, M., Newbold, D., Newcomer, M., Nichol, R., Nicolas-Arnaldos, F., Nikolica, A., Nikolov, J., Niner, E., Nishimura, K., Norman, A., Norrick, A., Novella, P., Nowak, A., Nowak, J. A., Oberling, M., Ochoa-Ricoux, J. P., Oh, S., Oh, S. B., Olivier, A., Olshevskiy, A., Olson, T., Onel, Y., Onishchuk, Y., Oranday, A., Gann, G. D. Orebi, Osbiston, M., Vélez, J. A. Osorio, O'Sullivan, L., Ormachea, L. Otiniano, Ott, J., Pagani, L., Palacio, G., Palamara, O., Palestini, S., Paley, J. M., Pallavicini, M., Palomares, C., Pan, S., Panda, P., Vazquez, W. Panduro, Pantic, E., Paolone, V., Papaleo, R., Papanestis, A., Papoulias, D., Paramesvaran, S., Paris, A., Parke, S., Parozzi, E., Parsa, S., Parsa, Z., Parveen, S., Parvu, M., Pasciuto, D., Pascoli, S., Pasqualini, L., Pasternak, J., Patrick, C., Patrizii, L., Patterson, R. B., Patzak, T., Paudel, A., Paulucci, L., Pavlovic, Z., Pawloski, G., Payne, D., Pec, V., Pedreschi, E., Peeters, S. J. M., Pellico, W., Perez, A. Pena, Pennacchio, E., Penzo, A., Peres, O. L. G., Gonzalez, Y. F. Perez, Pérez-Molina, L., Pernas, C., Perry, J., Pershey, D., Pessina, G., Petrillo, G., Petta, C., Petti, R., Pfaff, M., Pia, V., Pickering, L., Pietropaolo, F., Pimentel, V. L., Pinaroli, G., Pincha, S., Pinchault, J., Pitts, K., Plows, K., Pollack, C., Pollman, T., Pompa, F., Pons, X., Poonthottathil, N., Popov, V., Poppi, F., Porter, J., Paix{ã}o, L. G. Porto, Potekhin, M., Potenza, R., Pozimski, J., Pozzato, M., Prakash, T., Pratt, C., Prest, M., Psihas, F., Pugnere, D., Qian, X., Queen, J., Raaf, J. L., Radeka, V., Rademacker, J., Radics, B., Raffaelli, F., Rafique, A., Raguzin, E., Rai, M., Rajagopalan, S., Rajaoalisoa, M., Rakhno, I., Rakotondravohitra, L., Ralte, L., Delgado, M. A. Ramirez, Ramson, B., Rappoldi, A., Raselli, G., Ratoff, P., Ray, R., Razafinime, H., Rea, E. M., Real, J. S., Rebel, B., Rechenmacher, R., Reichenbacher, J., Reitzner, S. D., Sfar, H. Rejeb, Renner, E., Renshaw, A., Rescia, S., Resnati, F., Diego~Restrepo, Reynolds, C., Ribas, M., Riboldi, S., Riccio, C., Riccobene, G., Ricol, J. S., Rigan, M., Rincón, E. V., Ritchie-Yates, A., Ritter, S., Rivera, D., Rivera, R., Robert, A., Rocha, J. L. Rocabado, Rochester, L., Roda, M., Rodrigues, P., Alonso, M. J. Rodriguez, Rondon, J. Rodriguez, Rosauro-Alcaraz, S., Rosier, P., Ross, D., Rossella, M., Rossi, M., Ross-Lonergan, M., Roy, N., Roy, P., Rubbia, C., Ruggeri, A., Ruiz, G., Russell, B., Ruterbories, D., Rybnikov, A., Sacerdoti, S., Saha, S., Sahoo, S. K., Sahu, N., Sala, P., Samios, N., Samoylov, O., Sanchez, M. C., Bravo, A. Sánchez, Sánchez-Castillo, A., Sanchez-Lucas, P., Sandberg, V., Sanders, D. A., Sanfilippo, S., Sankey, D., Santoro, D., Saoulidou, N., Sapienza, P., Sarasty, C., Sarcevic, I., Sarra, I., Savage, G., Savinov, V., Scanavini, G., Scaramelli, A., Scarff, A., Schefke, T., Schellman, H., Schifano, S., Schlabach, P., Schmitz, D., Schneider, A. W., Scholberg, K., Schukraft, A., Schuld, B., Segade, A., Segreto, E., Selyunin, A., Senadheera, D., Senise, C. R., Sensenig, J., Seo, S. H., Shaevitz, M. H., Shanahan, P., Sharma, P., Kumar, R., Poudel, S. Sharma, Shaw, K., Shaw, T., Shchablo, K., Shen, J., Shepherd-Themistocleous, C., Sheshukov, A., Shi, J., Shi, W., Shin, S., Shivakoti, S., Shoemaker, I., Shooltz, D., Shrock, R., Siddi, B., Siden, M., Silber, J., Simard, L., Sinclair, J., Sinev, G., Singh, J., Singh, L., Singh, P., Singh, V., Chauhan, S. Singh, Sipos, R., Sironneau, C., Sirri, G., Siyeon, K., Skarpaas, K., Smedley, J., Smith, E., Smith, J., Smith, P., Smolik, J., Smy, M., Snape, M., Snider, E. L., Snopok, P., Snowden-Ifft, D., Nunes, M. Soares, Sobel, H., Soderberg, M., Sokolov, S., Salinas, C. J. Solano, Söldner-Rembold, S., Solomey, N., Solovov, V., Sondheim, W. E., Sorel, M., Sotnikov, A., Soto-Oton, J., Sousa, A., Soustruznik, K., Spinella, F., Spitz, J., Spooner, N. J. C., Spurgeon, K., Stalder, D., Stancari, M., Stanco, L., Steenis, J., Stein, R., Steiner, H. M., Lisbôa, A. F. Steklain, Stepanova, A., Stewart, J., Stillwell, B., Stock, J., Stocker, F., Stokes, T., Strait, M., Strauss, T., Strigari, L., Stuart, A., Suarez, J. G., Subash, J., Surdo, A., Suter, L., Sutera, C. M., Sutton, K., Suvorov, Y., Svoboda, R., Swain, S. K., Szczerbinska, B., Szelc, A. M., Sztuc, A., Taffara, A., Talukdar, N., Tamara, J., Tanaka, H. A., Tang, S., Taniuchi, N., Casanova, A. M. Tapia, Oregui, B. Tapia, Tapper, A., Tariq, S., Tarpara, E., Tatar, E., Tayloe, R., Tedeschi, D., Teklu, A. M., Vidal, J. Tena, Tennessen, P., Tenti, M., Terao, K., Terranova, F., Testera, G., Thakore, T., Thea, A., Thomas, S., Thompson, A., Thorn, C., Timm, S. C., Tiras, E., Tishchenko, V., Todorović, N., Tomassetti, L., Tonazzo, A., Torbunov, D., Torti, M., Tortola, M., Tortorici, F., Tosi, N., Totani, D., Toups, M., Touramanis, C., Tran, D., Travaglini, R., Trevor, J., Triller, E., Trilov, S., Truchon, J., Truncali, D., Trzaska, W. H., Tsai, Y., Tsai, Y. -T., Tsamalaidze, Z., Tsang, K. V., Tsverava, N., Tu, S. Z., Tufanli, S., Tunnell, C., Turnberg, S., Turner, J., Tuzi, M., Tyler, J., Tyley, E., Tzanov, M., Uchida, M. A., González, J. Ureña, Urheim, J., Usher, T., Utaegbulam, H., Uzunyan, S., Vagins, M. R., Vahle, P., Valder, S., Valdiviesso, G. A., Valencia, E., Valentim, R., Vallari, Z., Vallazza, E., Valle, J. W. F., Van Berg, R., Van de Water, R. G., Forero, D. V., Vannozzi, A., Van Nuland-Troost, M., Varanini, F., Oliva, D. Vargas, Vasina, S., Vaughan, N., Vaziri, K., Vázquez-Ramos, A., Vega, J., Ventura, S., Verdugo, A., Vergani, S., Verzocchi, M., Vetter, K., Vicenzi, M., de Souza, H. Vieira, Vignoli, C., Vilela, C., Villa, E., Viola, S., Viren, B., Hernandez, A. P. Vizcaya, Vuong, Q., Waldron, A. V., Wallbank, M., Walsh, J., Walton, T., Wang, H., Wang, J., Wang, L., Wang, M. H. L. S., Wang, X., Wang, Y., Warburton, K., Warner, D., Warsame, L., Wascko, M. O., Waters, D., Watson, A., Wawrowska, K., Weber, A., Weber, C. M., Weber, M., Wei, H., Weinstein, A., Westerdale, S., Wetstein, M., Whalen, K., White, A., Whitehead, L. H., Whittington, D., Wilhlemi, J., Wilking, M. J., Wilkinson, A., Wilkinson, C., Wilson, F., Wilson, R. J., Winter, P., Wisniewski, W., Wolcott, J., Wolfs, J., Wongjirad, T., Wood, A., Wood, K., Worcester, E., Worcester, M., Wospakrik, M., Wresilo, K., Wret, C., Wu, S., Wu, W., Wurm, M., Wyenberg, J., Xiao, Y., Xiotidis, I., Yaeggy, B., Yahlali, N., Yandel, E., Yang, J., Yang, K., Yang, T., Yankelevich, A., Yershov, N., Yonehara, K., Young, T., Yu, B., Yu, H., Yu, J., Yu, Y., Yuan, W., Zaki, R., Zalesak, J., Zambelli, L., Zamorano, B., Zani, A., Zapata, O., Zazueta, L., Zeller, G. P., Zennamo, J., Zeug, K., Zhang, C., Zhang, S., Zhao, M., Zhivun, E., Zimmerman, E. D., Zucchelli, S., Zuklin, J., Zutshi, V., and Zwaska, R.
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Physics - Instrumentation and Detectors ,High Energy Physics - Experiment - Abstract
The international collaboration designing and constructing the Deep Underground Neutrino Experiment (DUNE) at the Long-Baseline Neutrino Facility (LBNF) has developed a two-phase strategy toward the implementation of this leading-edge, large-scale science project. The 2023 report of the US Particle Physics Project Prioritization Panel (P5) reaffirmed this vision and strongly endorsed DUNE Phase I and Phase II, as did the European Strategy for Particle Physics. While the construction of the DUNE Phase I is well underway, this White Paper focuses on DUNE Phase II planning. DUNE Phase-II consists of a third and fourth far detector (FD) module, an upgraded near detector complex, and an enhanced 2.1 MW beam. The fourth FD module is conceived as a "Module of Opportunity", aimed at expanding the physics opportunities, in addition to supporting the core DUNE science program, with more advanced technologies. This document highlights the increased science opportunities offered by the DUNE Phase II near and far detectors, including long-baseline neutrino oscillation physics, neutrino astrophysics, and physics beyond the standard model. It describes the DUNE Phase II near and far detector technologies and detector design concepts that are currently under consideration. A summary of key R&D goals and prototyping phases needed to realize the Phase II detector technical designs is also provided. DUNE's Phase II detectors, along with the increased beam power, will complete the full scope of DUNE, enabling a multi-decadal program of groundbreaking science with neutrinos.
- Published
- 2024
37. Scalable DAQ system operating the CHIPS-5 neutrino detector
- Author
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Rancurel, Belén Alonso, Cao, Son, Carroll, Thomas J., Castellan, Rhys, Catano-Mur, Erika, Cesar, John P., Coelho, João A. B., Dills, Patrick, Dodwell, Thomas, Edmondson, Jack, van Eijk, Daan, Fetterly, Quinn, Garbal, Zoé, Germani, Stefano, Gilpin, Thomas, Giraudo, Anthony, Habig, Alec, Hanuska, Daniel, Hausner, Harry, Hernandez, Wilson Y., Holin, Anna, Huang, Junting, Jones, Sebastian B., Karle, Albrecht, Kileff, George, Jenkins, Kai R., Kooijman, Paul, Kreymer, Arthur, LaFond, Gabe M., Lang, Karol, Lazar, Jeffrey P., Li, Rui, Liu, Kexin, Loving, David A., Mánek, Petr, Marshak, Marvin L., Meier, Jerry R., Miller, William, Nelson, Jeffrey K., Ng, Christopher, Nichol, Ryan J., Paolone, Vittorio, Perch, Andrew, Pfützner, Maciej M., Radovic, Alexander, Rawlins, Katherine, Roedl, Patrick, Rogers, Lucas, Safa, Ibrahim, Sousa, Alexandre, Tingey, Josh, Thomas, Jennifer, Trokan-Tenorio, Jozef, Vahle, Patricia, Wade, Richard, Wendt, Christopher, Wendt, Daniel, Whitehead, Leigh H., Wolcott, Samuel, and Yuan, Tianlu
- Subjects
Physics - Instrumentation and Detectors - Abstract
The CHIPS R&D project focuses on development of low-cost water Cherenkov neutrino detectors through novel design strategies and resourceful engineering. This work presents an end-to-end DAQ solution intended for a recent 5 kt CHIPS prototype, which is largely based on affordable mass-produced components. Much like the detector itself, the presented instrumentation is composed of modular arrays that can be scaled up and easily serviced. A single such array can carry up to 30 photomultiplier tubes (PMTs) accompanied by electronics that generate high voltage in-situ and deliver time resolution of up to 0.69 ns. In addition, the technology is compatible with the White Rabbit timing system, which can synchronize its elements to within 100 ps. While deployment issues did not permit the presented DAQ system to operate beyond initial evaluation, the presented hardware and software successfully passed numerous commissioning tests that demonstrated their viability for use in a large-scale neutrino detector, instrumented with thousands of PMTs., Comment: 30 pages, 28 figures, submitted to MDPI Applied Sciences, Special Issue: Advanced Neutrino Detector Development and Application
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- 2024
38. First Measurement of the Total Inelastic Cross-Section of Positively-Charged Kaons on Argon at Energies Between 5.0 and 7.5 GeV
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DUNE Collaboration, Abud, A. Abed, Abi, B., Acciarri, R., Acero, M. A., Adames, M. R., Adamov, G., Adamowski, M., Adams, D., Adinolfi, M., Adriano, C., Aduszkiewicz, A., Aguilar, J., Akbar, F., Allison, K., Monsalve, S. Alonso, Alrashed, M., Alton, A., Alvarez, R., Alves, T., Amar, H., Amedo, P., Anderson, J., Andreopoulos, C., Andreotti, M., Andrews, M. P., Andrianala, F., Andringa, S., Anfimov, N., Ankowski, A., Antic, D., Antoniassi, M., Antonova, M., Antoshkin, A., Aranda-Fernandez, A., Arellano, L., Diaz, E. Arrieta, Arroyave, M. A., Asaadi, J., Ashkenazi, A., Asner, D., Asquith, L., Atkin, E., Auguste, D., Aurisano, A., Aushev, V., Autiero, D., Azam, M. B., Azfar, F., Back, A., Back, H., Back, J. J., Bagaturia, I., Bagby, L., Balashov, N., Balasubramanian, S., Baldi, P., Baldini, W., Baldonedo, J., Baller, B., Bambah, B., Banerjee, R., Barao, F., Barbu, D., Barenboim, G., Barham~Alzás, P., Barker, G. J., Barkhouse, W., Barr, G., Monarca, J. Barranco, Barros, A., Barros, N., Barrow, D., Barrow, J. L., Basharina-Freshville, A., Bashyal, A., Basque, V., Batchelor, C., Bathe-Peters, L., Battat, J. B. R., Battisti, F., Bay, F., Bazetto, M. C. Q., Alba, J. L. L. Bazo, Beacom, J. F., Bechetoille, E., Behera, B., Belchior, E., Bell, G., Bellantoni, L., Bellettini, G., Bellini, V., Beltramello, O., Benekos, N., Montiel, C. Benitez, Benjamin, D., Neves, F. Bento, Berger, J., Berkman, S., Bernal, J., Bernardini, P., Bersani, A., Bertolucci, S., Betancourt, M., Rodríguez, A. Betancur, Bevan, A., Bezawada, Y., Bezerra, A. T., Bezerra, T. J., Bhat, A., Bhatnagar, V., Bhatt, J., Bhattacharjee, M., Bhattacharya, M., Bhuller, S., Bhuyan, B., Biagi, S., Bian, J., Biery, K., Bilki, B., Bishai, M., Bitadze, A., Blake, A., Blaszczyk, F. D., Blazey, G. C., Blucher, E., Bodek, A., Bogenschuetz, J., Boissevain, J., Bolognesi, S., Bolton, T., Bomben, L., Bonesini, M., Bonilla-Diaz, C., Bonini, F., Booth, A., Boran, F., Bordoni, S., Merlo, R. Borges, Borkum, A., Bostan, N., Bouet, R., Boza, J., Bracinik, J., Brahma, B., Brailsford, D., Bramati, F., Branca, A., Brandt, A., Bremer, J., Brew, C., Brice, S. J., Brio, V., Brizzolari, C., Bromberg, C., Brooke, J., Bross, A., Brunetti, G., Brunetti, M., Buchanan, N., Budd, H., Buergi, J., Bundock, A., Burgardt, D., Butchart, S., V., G. Caceres, Cagnoli, I., Cai, T., Calabrese, R., Calcutt, J., Calivers, L., Calvo, E., Caminata, A., Camino, A. F., Campanelli, W., Campani, A., Benitez, A. Campos, Canci, N., Capó, J., Caracas, I., Caratelli, D., Carber, D., Carceller, J. M., Carini, G., Carlus, B., Carneiro, M. F., Carniti, P., Terrazas, I. Caro, Carranza, H., Carrara, N., Carroll, L., Carroll, T., Carter, A., Casarejos, E., Casazza, D., Forero, J. F. Castaño, Castaño, F. A., Castillo, A., Castromonte, C., Catano-Mur, E., Cattadori, C., Cavalier, F., Cavanna, F., Centro, S., Cerati, G., Cerna, C., Cervelli, A., Villanueva, A. Cervera, Chakraborty, K., Chakraborty, S., Chalifour, M., Chappell, A., Charitonidis, N., Chatterjee, A., Chen, H., Chen, M., Chen, W. C., Chen, Y., Chen-Wishart, Z., Cherdack, D., Chi, C., Chiapponi, F., Chirco, R., Chitirasreemadam, N., Cho, K., Choate, S., Chokheli, D., Chong, P. S., Chowdhury, B., Christian, D., Chukanov, A., Chung, M., Church, E., Cicala, M. F., Cicerchia, M., Cicero, V., Ciolini, R., Clarke, P., Cline, G., Coan, T. E., Cocco, A. G., Coelho, J. A. B., Cohen, A., Collazo, J., Collot, J., Conley, E., Conrad, J. M., Convery, M., Copello, S., Cova, P., Cox, C., Cremaldi, L., Cremonesi, L., Crespo-Anadón, J. I., Crisler, M., Cristaldo, E., Crnkovic, J., Crone, G., Cross, R., Cudd, A., Cuesta, C., Cui, Y., Curciarello, F., Cussans, D., Dai, J., Dalager, O., Dallavalle, R., Dallaway, W., D'Amico, R., da Motta, H., Dar, Z. A., Darby, R., Peres, L. Da Silva, David, Q., Davies, G. S., Davini, S., Dawson, J., De Aguiar, R., De Almeida, P., Debbins, P., De Bonis, I., Decowski, M. P., de Gouvêa, A., De Holanda, P. C., Astiz, I. L. De Icaza, De Jong, P., Sanchez, P. Del Amo, De la Torre, A., De Lauretis, G., Delbart, A., Delepine, D., Delgado, M., Dell'Acqua, A., Monache, G. Delle, Delmonte, N., De Lurgio, P., Demario, R., De Matteis, G., Neto, J. R. T. de Mello, DeMuth, D. M., Dennis, S., Densham, C., Denton, P., Deptuch, G. W., De Roeck, A., De Romeri, V., Detje, J. P., Devine, J., Dharmapalan, R., Dias, M., Diaz, A., Díaz, J. S., Díaz, F., Di Capua, F., Di Domenico, A., Di Domizio, S., Di Falco, S., Di Giulio, L., Ding, P., Di Noto, L., Diociaiuti, E., Distefano, C., Diurba, R., Diwan, M., Djurcic, Z., Doering, D., Dolan, S., Dolek, F., Dolinski, M. J., Domenici, D., Domine, L., Donati, S., Donon, Y., Doran, S., Douglas, D., Doyle, T. A., Dragone, A., Drielsma, F., Duarte, L., Duchesneau, D., Duffy, K., Dugas, K., Dunne, P., Dutta, B., Duyang, H., Dwyer, D. A., Dyshkant, A. S., Dytman, S., Eads, M., Earle, A., Edayath, S., Edmunds, D., Eisch, J., Englezos, P., Ereditato, A., Erjavec, T., Escobar, C. O., Evans, J. J., Ewart, E., Ezeribe, A. C., Fahey, K., Fajt, L., Falcone, A., Fani', M., Farnese, C., Farrell, S., Farzan, Y., Fedoseev, D., Felix, J., Feng, Y., Fernandez-Martinez, E., Ferry, G., Fialova, E., Fields, L., Filip, P., Filkins, A., Filthaut, F., Fine, R., Fiorillo, G., Fiorini, M., Fogarty, S., Foreman, W., Fowler, J., Franc, J., Francis, K., Franco, D., Franklin, J., Freeman, J., Fried, J., Friedland, A., Fuess, S., Furic, I. K., Furman, K., Furmanski, A. P., Gaba, R., Gabrielli, A., M~Gago, A., Galizzi, F., Gallagher, H., Gallice, N., Galymov, V., Gamberini, E., Gamble, T., Ganacim, F., Gandhi, R., Ganguly, S., Gao, F., Gao, S., Garcia-Gamez, D., García-Peris, M. Á., Gardim, F., Gardiner, S., Gastler, D., Gauch, A., Gauvreau, J., Gauzzi, P., Gazzana, S., Ge, G., Geffroy, N., Gelli, B., Gent, S., Gerlach, L., Ghorbani-Moghaddam, Z., Giammaria, T., Gibin, D., Gil-Botella, I., Gilligan, S., Gioiosa, A., Giovannella, S., Girerd, C., Giri, A. K., Giugliano, C., Giusti, V., Gnani, D., Gogota, O., Gollapinni, S., Gollwitzer, K., Gomes, R. A., Bermeo, L. V. Gomez, Fajardo, L. S. Gomez, Gonnella, F., Gonzalez-Diaz, D., Gonzalez-Lopez, M., Goodman, M. C., Goswami, S., Gotti, C., Goudeau, J., Goudzovski, E., Grace, C., Gramellini, E., Gran, R., Granados, E., Granger, P., Grant, C., Gratieri, D. R., Grauso, G., Green, P., Greenberg, S., Greer, J., Griffith, W. C., Groetschla, F. T., Grzelak, K., Gu, L., Gu, W., Guarino, V., Guarise, M., Guenette, R., Guerzoni, M., Guffanti, D., Guglielmi, A., Guo, B., Guo, F. Y., Gupta, A., Gupta, V., Gurung, G., Gutierrez, D., Guzowski, P., Guzzo, M. M., Gwon, S., Habig, A., Hadavand, H., Haegel, L., Haenni, R., Hagaman, L., Hahn, A., Haiston, J., Hakenmüller, J., Hamernik, T., Hamilton, P., Hancock, J., Happacher, F., Harris, D. A., Hartnell, J., Hartnett, T., Harton, J., Hasegawa, T., Hasnip, C. M., Hatcher, R., Hayrapetyan, K., Hays, J., Hazen, E., He, M., Heavey, A., Heeger, K. M., Heise, J., Hellmuth, P., Henry, S., Herner, K., Hewes, V., Higuera, A., Hilgenberg, C., Hillier, S. J., Himmel, A., Hinkle, E., Hirsch, L. R., Ho, J., Hoff, J., Holin, A., Holvey, T., Hoppe, E., Horiuchi, S., Horton-Smith, G. A., Houdy, T., Howard, B., Howell, R., Hristova, I., Hronek, M. S., Huang, J., Huang, R. G., Hulcher, Z., Ibrahim, M., Iles, G., Ilic, N., Iliescu, A. M., Illingworth, R., Ingratta, G., Ioannisian, A., Irwin, B., Isenhower, L., Oliveira, M. Ismerio, Itay, R., Jackson, C. M., Jain, V., James, E., Jang, W., Jargowsky, B., Jena, D., Jentz, I., Ji, X., Jiang, C., Jiang, J., Jiang, L., Jipa, A., Jo, J. H., Joaquim, F. R., Johnson, W., Jollet, C., Jones, B., Jones, R., Jovancevic, N., Judah, M., Jung, C. K., Junk, T., Jwa, Y., Kabirnezhad, M., Kaboth, A. C., Kadenko, I., Kakorin, I., Kalitkina, A., Kalra, D., Kandemir, M., Kaplan, D. M., Karagiorgi, G., Karaman, G., Karcher, A., Karyotakis, Y., Kasai, S., Kasetti, S. P., Kashur, L., Katsioulas, I., Kauther, A., Kazaryan, N., Ke, L., Kearns, E., Keener, P. T., Kelly, K. J., Kemp, E., Kemularia, O., Kermaidic, Y., Ketchum, W., Kettell, S. H., Khabibullin, M., Khan, N., Khvedelidze, A., Kim, D., Kim, J., Kim, M. J., King, B., Kirby, B., Kirby, M., Kish, A., Klein, J., Kleykamp, J., Klustova, A., Kobilarcik, T., Koch, L., Koehler, K., Koerner, L. W., Koh, D. H., Kolupaeva, L., Korablev, D., Kordosky, M., Kosc, T., Kose, U., Kostelecký, V. A., Kothekar, K., Kotler, I., Kovalcuk, M., Kozhukalov, V., Krah, W., Kralik, R., Kramer, M., Kreczko, L., Krennrich, F., Kreslo, I., Kroupova, T., Kubota, S., Kubu, M., Kudenko, Y., Kudryavtsev, V. A., Kufatty, G., Kuhlmann, S., Kulagin, S., Kumar, J., Kumar, P., Kumaran, S., Kunzmann, J., Kuravi, R., Kurita, N., Kuruppu, C., Kus, V., Kutter, T., Kvasnicka, J., Labree, T., Lackey, T., Lal{ă}u, I., Lambert, A., Land, B. J., Lane, C. E., Lane, N., Lang, K., Langford, T., Langstaff, M., Lanni, F., Lantwin, O., Larkin, J., Lasorak, P., Last, D., Laudrain, A., Laundrie, A., Laurenti, G., Lavaut, E., Laycock, P., Lazanu, I., LaZur, R., Lazzaroni, M., Le, T., Leardini, S., Learned, J., LeCompte, T., Legin, V., Miotto, G. Lehmann, Lehnert, R., de Oliveira, M. A. Leigui, Leitner, M., Silverio, D. Leon, Lepin, L. M., -Y~Li, J., Li, S. W., Li, Y., Liao, H., Lin, C. S., Lindebaum, D., Linden, S., Lineros, R. A., Lister, A., Littlejohn, B. R., Liu, H., Liu, J., Liu, Y., Lockwitz, S., Lokajicek, M., Lomidze, I., Long, K., Lopes, T. V., Lopez, J., de Rego, I. López, López-March, N., Lord, T., LoSecco, J. M., Louis, W. C., Sanchez, A. Lozano, Lu, X. -G., Luk, K. B., Lunday, B., Luo, X., Luppi, E., MacFarlane, D., Machado, A. A., Machado, P., Macias, C. T., Macier, J. R., MacMahon, M., Maddalena, A., Madera, A., Madigan, P., Magill, S., Magueur, C., Mahn, K., Maio, A., Major, A., Majumdar, K., Mameli, S., Man, M., Mandujano, R. C., Maneira, J., Manly, S., Mann, A., Manolopoulos, K., Plata, M. Manrique, Corchado, S. Manthey, Manyam, V. N., Marchan, M., Marchionni, A., Marciano, W., Marfatia, D., Mariani, C., Maricic, J., Marinho, F., Marino, A. D., Markiewicz, T., Marques, F. Das Chagas, Marquet, C., Marshak, M., Marshall, C. M., Marshall, J., Martina, L., Martín-Albo, J., Martinez, N., Caicedo, D. A. Martinez, López, F. Martínez, Miravé, P. Martínez, Martynenko, S., Mascagna, V., Massari, C., Mastbaum, A., Matichard, F., Matsuno, S., Matteucci, G., Matthews, J., Mauger, C., Mauri, N., Mavrokoridis, K., Mawby, I., Mazza, R., McAskill, T., McConkey, N., McFarland, K. S., McGrew, C., McNab, A., Meazza, L., Meddage, V. C. N., Mefodiev, A., Mehta, B., Mehta, P., Melas, P., Mena, O., Mendez, H., Mendez, P., Méndez, D. P., Menegolli, A., Meng, G., Mercuri, A. C. E. A., Meregaglia, A., Messier, M. D., Metallo, S., Metcalf, W., Mewes, M., Meyer, H., Miao, T., Micallef, J., Miccoli, A., Michna, G., Milincic, R., Miller, F., Miller, G., Miller, W., Mineev, O., Minotti, A., Miralles, L., Miranda, O. G., Mironov, C., Miryala, S., Miscetti, S., Mishra, C. S., Mishra, P., Mishra, S. R., Mislivec, A., Mitchell, M., Mladenov, D., Mocioiu, I., Mogan, A., Moggi, N., Mohanta, R., Mohayai, T. A., Mokhov, N., Molina, J., Bueno, L. Molina, Montagna, E., Montanari, A., Montanari, C., Montanari, D., Montanino, D., Zetina, L. M. Montaño, Mooney, M., Moor, A. F., Moore, Z., Moreno, D., Moreno-Palacios, O., Morescalchi, L., Moretti, D., Moretti, R., Morris, C., Mossey, C., Moura, C. A., Mouster, G., Mu, W., Mualem, L., Mueller, J., Muether, M., Muheim, F., Muir, A., Mulhearn, M., Munford, D., Munteanu, L. J., Muramatsu, H., Muraz, J., Murphy, M., Murphy, T., Muse, J., Mytilinaki, A., Nachtman, J., Nagai, Y., Nagu, S., Nandakumar, R., Naples, D., Narita, S., Navrer-Agasson, A., Nayak, N., Nebot-Guinot, M., Nehm, A., Nelson, J. K., Neogi, O., Nesbit, J., Nessi, M., Newbold, D., Newcomer, M., Nichol, R., Nicolas-Arnaldos, F., Nikolica, A., Nikolov, J., Niner, E., Nishimura, K., Norman, A., Norrick, A., Novella, P., Nowak, A., Nowak, J. A., Oberling, M., Ochoa-Ricoux, J. P., Oh, S., Oh, S. B., Olivier, A., Olshevskiy, A., Olson, T., Onel, Y., Onishchuk, Y., Oranday, A., Osbiston, M., Vélez, J. A. Osorio, O'Sullivan, L., Ormachea, L. Otiniano, Ott, J., Pagani, L., Palacio, G., Palamara, O., Palestini, S., Paley, J. M., Pallavicini, M., Palomares, C., Pan, S., Panda, P., Vazquez, W. Panduro, Pantic, E., Paolone, V., Papaleo, R., Papanestis, A., Papoulias, D., Paramesvaran, S., Paris, A., Parke, S., Parozzi, E., Parsa, S., Parsa, Z., Parveen, S., Parvu, M., Pasciuto, D., Pascoli, S., Pasqualini, L., Pasternak, J., Patrick, C., Patrizii, L., Patterson, R. B., Patzak, T., Paudel, A., Paulucci, L., Pavlovic, Z., Pawloski, G., Payne, D., Pec, V., Pedreschi, E., Peeters, S. J. M., Pellico, W., Perez, A. Pena, Pennacchio, E., Penzo, A., Peres, O. L. G., Gonzalez, Y. F. Perez, Pérez-Molina, L., Pernas, C., Perry, J., Pershey, D., Pessina, G., Petrillo, G., Petta, C., Petti, R., Pfaff, M., Pia, V., Pickering, L., Pietropaolo, F., Pimentel, V. L., Pinaroli, G., Pincha, S., Pinchault, J., Pitts, K., Plows, K., Pollack, C., Pollman, T., Pompa, F., Pons, X., Poonthottathil, N., Popov, V., Poppi, F., Porter, J., Paix{ã}o, L. G. Porto, Potekhin, M., Potenza, R., Pozimski, J., Pozzato, M., Prakash, T., Pratt, C., Prest, M., Psihas, F., Pugnere, D., Qian, X., Queen, J., Raaf, J. 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- Subjects
High Energy Physics - Experiment ,Physics - Instrumentation and Detectors - Abstract
ProtoDUNE Single-Phase (ProtoDUNE-SP) is a 770-ton liquid argon time projection chamber that operated in a hadron test beam at the CERN Neutrino Platform in 2018. We present a measurement of the total inelastic cross section of charged kaons on argon as a function of kaon energy using 6 and 7 GeV/$c$ beam momentum settings. The flux-weighted average of the extracted inelastic cross section at each beam momentum setting was measured to be 380$\pm$26 mbarns for the 6 GeV/$c$ setting and 379$\pm$35 mbarns for the 7 GeV/$c$ setting.
- Published
- 2024
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39. Supernova Pointing Capabilities of DUNE
- Author
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DUNE Collaboration, Abud, A. Abed, Abi, B., Acciarri, R., Acero, M. A., Adames, M. R., Adamov, G., Adamowski, M., Adams, D., Adinolfi, M., Adriano, C., Aduszkiewicz, A., Aguilar, J., Aimard, B., Akbar, F., Allison, K., Monsalve, S. Alonso, Alrashed, M., Alton, A., Alvarez, R., Alves, T., Amar, H., Amedo, P., Anderson, J., Andrade, D. A., Andreopoulos, C., Andreotti, M., Andrews, M. P., Andrianala, F., Andringa, S., Anfimov, N., Ankowski, A., Antoniassi, M., Antonova, M., Antoshkin, A., Aranda-Fernandez, A., Arellano, L., Diaz, E. Arrieta, Arroyave, M. A., Asaadi, J., Ashkenazi, A., Asner, D., Asquith, L., Atkin, E., Auguste, D., Aurisano, A., Aushev, V., Autiero, D., Azfar, F., Back, A., Back, H., Back, J. J., Bagaturia, I., Bagby, L., Balashov, N., Balasubramanian, S., Baldi, P., Baldini, W., Baldonedo, J., Baller, B., Bambah, B., Banerjee, R., Barao, F., Barenboim, G., Alzás, P. Barham, Barker, G. J., Barkhouse, W., Barr, G., Monarca, J. 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J., Muramatsu, H., Muraz, J., Murphy, M., Murphy, T., Muse, J., Mytilinaki, A., Nachtman, J., Nagai, Y., Nagu, S., Nandakumar, R., Naples, D., Narita, S., Nath, A., Navrer-Agasson, A., Nayak, N., Nebot-Guinot, M., Nehm, A., Nelson, J. K., Neogi, O., Nesbit, J., Nessi, M., Newbold, D., Newcomer, M., Nichol, R., Nicolas-Arnaldos, F., Nikolica, A., Nikolov, J., Niner, E., Nishimura, K., Norman, A., Norrick, A., Novella, P., Nowak, J. A., Oberling, M., Ochoa-Ricoux, J. P., Oh, S., Oh, S. B., Olivier, A., Olshevskiy, A., Olson, T., Onel, Y., Onishchuk, Y., Oranday, A., Osbiston, M., Vélez, J. A. Osorio, Ormachea, L. Otiniano, Ott, J., Pagani, L., Palacio, G., Palamara, O., Palestini, S., Paley, J. M., Pallavicini, M., Palomares, C., Pan, S., Panda, P., Vazquez, W. Panduro, Pantic, E., Paolone, V., Papadimitriou, V., Papaleo, R., Papanestis, A., Papoulias, D., Paramesvaran, S., Paris, A., Parke, S., Parozzi, E., Parsa, S., Parsa, Z., Parveen, S., Parvu, M., Pasciuto, D., Pascoli, S., Pasqualini, L., Pasternak, J., Patrick, C., Patrizii, L., Patterson, R. B., Patzak, T., Paudel, A., Paulucci, L., Pavlovic, Z., Pawloski, G., Payne, D., Pec, V., Pedreschi, E., Peeters, S. J. M., Pellico, W., Perez, A. Pena, Pennacchio, E., Penzo, A., Peres, O. L. G., Gonzalez, Y. F. Perez, Pérez-Molina, L., Pernas, C., Perry, J., Pershey, D., Pessina, G., Petrillo, G., Petta, C., Petti, R., Pfaff, M., Pia, V., Pickering, L., Pietropaolo, F., Pimentel, V. L., Pinaroli, G., Pinchault, J., Pitts, K., Plows, K., Plunkett, R., Pollack, C., Pollman, T., Polo-Toledo, D., Pompa, F., Pons, X., Poonthottathil, N., Popov, V., Poppi, F., Porter, J., Potekhin, M., Potenza, R., Pozimski, J., Pozzato, M., Prakash, T., Pratt, C., Prest, M., Psihas, F., Pugnere, D., Qian, X., Queen, J., Raaf, J. L., Radeka, V., Rademacker, J., Radics, B., Rafique, A., Raguzin, E., Rai, M., Rajagopalan, S., Rajaoalisoa, M., Rakhno, I., Rakotondravohitra, L., Ralte, L., Delgado, M. A. Ramirez, Ramson, B., Rappoldi, A., Raselli, G., Ratoff, P., Ray, R., Razafinime, H., Rea, E. M., Real, J. S., Rebel, B., Rechenmacher, R., Reggiani-Guzzo, M., Reichenbacher, J., Reitzner, S. D., Sfar, H. Rejeb, Renner, E., Renshaw, A., Rescia, S., Resnati, F., Restrepo, Diego, Reynolds, C., Ribas, M., Riboldi, S., Riccio, C., Riccobene, G., Ricol, J. S., Rigan, M., Rincón, E. V., Ritchie-Yates, A., Ritter, S., Rivera, D., Rivera, R., Robert, A., Rocha, J. L. Rocabado, Rochester, L., Roda, M., Rodrigues, P., Alonso, M. J. Rodriguez, Roeth, A. J., Rondon, J. Rodriguez, Rosauro-Alcaraz, S., Rosier, P., Ross, D., Rossella, M., Rossi, M., Ross-Lonergan, M., Roy, N., Roy, P., Rubbia, C., Ruggeri, A., Ferreira, G. Ruiz, Russell, B., Ruterbories, D., Rybnikov, A., Saa-Hernandez, A., Saakyan, R., Sacerdoti, S., Sahoo, S. K., Sahu, N., Sala, P., Samios, N., Samoylov, O., Sanchez, M. C., Bravo, A. Sánchez, Sanchez-Lucas, P., Sandberg, V., Sanders, D. A., Sanfilippo, S., Sankey, D., Santoro, D., Saoulidou, N., Sapienza, P., Sarasty, C., Sarcevic, I., Sarra, I., Savage, G., Savinov, V., Scanavini, G., Scaramelli, A., Scarff, A., Schefke, T., Schellman, H., Schifano, S., Schlabach, P., Schmitz, D., Schneider, A. W., Scholberg, K., Schukraft, A., Schuld, B., Segade, A., Segreto, E., Selyunin, A., Senise, C. R., Sensenig, J., Shaevitz, M. H., Shanahan, P., Sharma, P., Kumar, R., Shaw, K., Shaw, T., Shchablo, K., Shen, J., Shepherd-Themistocleous, C., Sheshukov, A., Shi, W., Shin, S., Shivakoti, S., Shoemaker, I., Shooltz, D., Shrock, R., Siddi, B., Siden, M., Silber, J., Simard, L., Sinclair, J., Sinev, G., Singh, Jaydip, Singh, J., Singh, L., Singh, P., Singh, V., Chauhan, S. Singh, Sipos, R., Sironneau, C., Sirri, G., Siyeon, K., Skarpaas, K., Smedley, J., Smith, E., Smith, J., Smith, P., Smolik, J., Smy, M., Snape, M., Snider, E. L., Snopok, P., Snowden-Ifft, D., Nunes, M. Soares, Sobel, H., Soderberg, M., Sokolov, S., Salinas, C. J. Solano, Söldner-Rembold, S., Soleti, S. R., Solomey, N., Solovov, V., Sondheim, W. E., Sorel, M., Sotnikov, A., Soto-Oton, J., Sousa, A., Soustruznik, K., Spinella, F., Spitz, J., Spooner, N. J. C., Spurgeon, K., Stalder, D., Stancari, M., Stanco, L., Steenis, J., Stein, R., Steiner, H. M., Lisbôa, A. F. Steklain, Stepanova, A., Stewart, J., Stillwell, B., Stock, J., Stocker, F., Stokes, T., Strait, M., Strauss, T., Strigari, L., Stuart, A., Suarez, J. G., Subash, J., Surdo, A., Suter, L., Sutera, C. M., Sutton, K., Suvorov, Y., Svoboda, R., Swain, S. K., Szczerbinska, B., Szelc, A. M., Sztuc, A., Taffara, A., Talukdar, N., Tamara, J., Tanaka, H. A., Tang, S., Taniuchi, N., Casanova, A. M. Tapia, Oregui, B. Tapia, Tapper, A., Tariq, S., Tarpara, E., Tatar, E., Tayloe, R., Tedeschi, D., Teklu, A. M., Vidal, J. Tena, Tennessen, P., Tenti, M., Terao, K., Terranova, F., Testera, G., Thakore, T., Thea, A., Thiebault, A., Thomas, S., Thompson, A., Thorn, C., Timm, S. C., Tiras, E., Tishchenko, V., Todorović, N., Tomassetti, L., Tonazzo, A., Torbunov, D., Torti, M., Tortola, M., Tortorici, F., Tosi, N., Totani, D., Toups, M., Touramanis, C., Tran, D., Travaglini, R., Trevor, J., Triller, E., Trilov, S., Truchon, J., Truncali, D., Trzaska, W. H., Tsai, Y., Tsai, Y. -T., Tsamalaidze, Z., Tsang, K. V., Tsverava, N., Tu, S. Z., Tufanli, S., Tunnell, C., Turner, J., Tuzi, M., Tyler, J., Tyley, E., Tzanov, M., Uchida, M. A., González, J. Ureña, Urheim, J., Usher, T., Utaegbulam, H., Uzunyan, S., Vagins, M. R., Vahle, P., Valder, S., Valdiviesso, G. A., Valencia, E., Valentim, R., Vallari, Z., Vallazza, E., Valle, J. W. F., Van Berg, R., Van de Water, R. G., Forero, D. V., Vannozzi, A., Van Nuland-Troost, M., Varanini, F., Oliva, D. Vargas, Vasina, S., Vaughan, N., Vaziri, K., Vázquez-Ramos, A., Vega, J., Ventura, S., Verdugo, A., Vergani, S., Verzocchi, M., Vetter, K., Vicenzi, M., de Souza, H. Vieira, Vignoli, C., Vilela, C., Villa, E., Viola, S., Viren, B., Vizcaya-Hernandez, A., Vrba, T., Vuong, Q., Waldron, A. V., Wallbank, M., Walsh, J., Walton, T., Wang, H., Wang, J., Wang, L., Wang, M. H. L. S., Wang, X., Wang, Y., Warburton, K., Warner, D., Warsame, L., Wascko, M. O., Waters, D., Watson, A., Wawrowska, K., Weber, A., Weber, C. M., Weber, M., Wei, H., Weinstein, A., Wenzel, H., Westerdale, S., Wetstein, M., Whalen, K., Whilhelmi, J., White, A., Whitehead, L. H., Whittington, D., Wilking, M. J., Wilkinson, A., Wilkinson, C., Wilson, F., Wilson, R. J., Winter, P., Wisniewski, W., Wolcott, J., Wolfs, J., Wongjirad, T., Wood, A., Wood, K., Worcester, E., Worcester, M., Wospakrik, M., Wresilo, K., Wret, C., Wu, S., Wu, W., Wurm, M., Wyenberg, J., Xiao, Y., Xiotidis, I., Yaeggy, B., Yahlali, N., Yandel, E., Yang, K., Yang, T., Yankelevich, A., Yershov, N., Yonehara, K., Young, T., Yu, B., Yu, H., Yu, J., Yu, Y., Yuan, W., Zaki, R., Zalesak, J., Zambelli, L., Zamorano, B., Zani, A., Zapata, O., Zazueta, L., Zeller, G. P., Zennamo, J., Zeug, K., Zhang, C., Zhang, S., Zhao, M., Zhivun, E., Zimmerman, E. D., Zucchelli, S., Zuklin, J., Zutshi, V., and Zwaska, R.
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High Energy Physics - Experiment ,Astrophysics - High Energy Astrophysical Phenomena ,Astrophysics - Instrumentation and Methods for Astrophysics ,Astrophysics - Solar and Stellar Astrophysics ,Nuclear Experiment ,Physics - Instrumentation and Detectors - Abstract
The determination of the direction of a stellar core collapse via its neutrino emission is crucial for the identification of the progenitor for a multimessenger follow-up. A highly effective method of reconstructing supernova directions within the Deep Underground Neutrino Experiment (DUNE) is introduced. The supernova neutrino pointing resolution is studied by simulating and reconstructing electron-neutrino charged-current absorption on $^{40}$Ar and elastic scattering of neutrinos on electrons. Procedures to reconstruct individual interactions, including a newly developed technique called ``brems flipping'', as well as the burst direction from an ensemble of interactions are described. Performance of the burst direction reconstruction is evaluated for supernovae happening at a distance of 10 kpc for a specific supernova burst flux model. The pointing resolution is found to be 3.4 degrees at 68% coverage for a perfect interaction-channel classification and a fiducial mass of 40 kton, and 6.6 degrees for a 10 kton fiducial mass respectively. Assuming a 4% rate of charged-current interactions being misidentified as elastic scattering, DUNE's burst pointing resolution is found to be 4.3 degrees (8.7 degrees) at 68% coverage., Comment: 25 pages, 16 figures
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- 2024
40. The resident TP712 prophage of Lactococcus lactis MG1363 provides extra holin functions to the new P335 phage CAP for effective host lysis
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Agencia Estatal de Investigación (España), European Commission, Ministerio de Ciencia, Innovación y Universidades (España), Principado de Asturias, Rodríguez González, Ana [0000-0002-1577-9905], Martínez Fernández, Beatriz [0000-0001-7692-1963], Escobedo, Susana, Wegmann, Udo, Pérez de Pipaon, Mikel, Campelo, Ana B., Stentz, Régis, Rodríguez González, Ana, Martínez Fernández, Beatriz, Agencia Estatal de Investigación (España), European Commission, Ministerio de Ciencia, Innovación y Universidades (España), Principado de Asturias, Rodríguez González, Ana [0000-0002-1577-9905], Martínez Fernández, Beatriz [0000-0001-7692-1963], Escobedo, Susana, Wegmann, Udo, Pérez de Pipaon, Mikel, Campelo, Ana B., Stentz, Régis, Rodríguez González, Ana, and Martínez Fernández, Beatriz
- Abstract
Prophages are widely present in Lactococcus lactis, a lactic acid bacterium (LAB) that plays a key role in dairy fermentations. L. lactis MG1363 is a laboratory strain used worldwide as a model LAB. Initially regarded as plasmid- and prophage-free, MG1363 carries two complete prophages TP712 and MG-3. Only TP712 seems to be inducible but unable to lyse the host. Several so-called TP712 lysogens able to lyse upon prophage induction were reported in the past, but the reason for their lytic phenotype remained unknown. In this work, we describe CAP, a new P335 prophage detected in the “lytic TP712 lysogens”, which had remained unnoticed. CAP is able to excise after mitomycin C treatment, along with TP712, and able to infect L. lactis MG1363-like strains but not the lytic TP712 lysogens. Both phages cooperate for efficient host lysis. While the expression in trans of the CAP lytic genes was sufficient to trigger cell lysis, this process was boosted when the resident TP712 prophage was concomitantly induced. Introduction of mutations into the TP712 lytic genes revealed that its holin but not its endolysin plays a major role. Accordingly, it is shown that the lytic activity of the recombinant CAP endolysin relies on membrane depolarization. Revisiting the seminal work to generate the extensively used L. lactis MG1363 strain led us to conclude that the CAP phage was originally present in its ancestor L. lactis NCDO712 and our results solved long-standing mysteries around the MG1363 resident prophage TP712 reported in the “pre-sequencing” era.
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- 2021
41. A GH19 lysozyme and peptidase from Myoviridae cyanophages lacking the typical holin-endolysin system exhibit lytic activity
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Meng, Li-Hui, primary, Ke, Fei, additional, Zhang, Qi-Ya, additional, Hu, Ya-Dong, additional, and Zhao, Zhe, additional
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- 2023
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42. The TcdE holin drives toxin secretion and virulence in Clostridioides difficile.
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DiBenedetto, Nicholas Vincent, primary, Oberkampf, Marine, additional, Cersosimo, Laura, additional, Yeliseyev, Vladimir, additional, Bry, Lynn, additional, Peltier, Johann, additional, and Dupuy, Bruno, additional
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- 2023
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- View/download PDF
43. From Cell Death to Metabolism: Holin-Antiholin Homologues with New Functions
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Marielle H. van den Esker, Ákos T. Kovács, and Oscar P. Kuipers
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Bacillus subtilis ,Staphylococcus aureus ,antiholin ,evolution ,holin ,metabolism ,Microbiology ,QR1-502 - Abstract
ABSTRACT Programmed cell death in bacteria is generally triggered by membrane proteins with functions analogous to those of bacteriophage holins: they disrupt the membrane potential, whereas antiholins antagonize this process. The holin-like class of proteins is present in all three domains of life, but their functions can be different, depending on the species. Using a series of biochemical and genetic approaches, in a recent article in mBio, Charbonnier et al. (mBio 8:e00976-17, 2017, https://doi.org/10.1128/mBio.00976-17 ) demonstrate that the antiholin homologue in Bacillus subtilis transports pyruvate and is regulated in an unconventional way by its substrate molecule. Here, we discuss the connection between cell death and metabolism in various bacteria carrying genes encoding these holin-antiholin analogues and place the recent study by Charbonnier et al. in an evolutionary context.
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- 2017
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44. Holin triggering in real time
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White, Rebecca, Chiba, Shinobu, Pang, Ting, Dewey, Jill S., Savva, Christos G., Holzenburg, Andreas, Pogliano, Kit, Young, Ry, and Collier, R. John
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- 2011
45. Production of Lactobacillus plantarum ghosts by conditional expression of a prophage-encoded holin.
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Riangrungroj, Pinpunya, Visessanguan, Wonnop, and Leartsakulpanich, Ubolsree
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- *
LACTOBACILLUS plantarum , *GROWTH disorders , *BACTERIAL cells , *GRAM-positive bacteria , *PATHOGENIC bacteria , *CELL culture - Abstract
Bacterial ghosts (BGs) are nonviable empty bacterial cell envelopes with intact cellular morphology and native surface structure. BGs made from pathogenic bacteria are used for biomedical and pharmaceutical applications. However, incomplete pathogenic cell inactivation during BG preparation raises safety concerns that could limit the intended use. Therefore, safer bacterial cell types are needed for BG production. Here, we produced BGs from the food-grade Gram-positive bacterium Lactobacillus plantarum TBRC 2–4 by conditional expression of a prophage-encoded holin (LpHo). LpHo expression was regulated using the pheromone-inducible pSIP system and LpHo was localized to the cell membrane. Upon LpHo induction, a significant growth retardation and a drastic decrease in cell viability were observed. LpHo-induced cells also showed membrane pores by scanning electron microscopy, membrane depolarization by flow cytometry, and release of nucleic acid contents in the cell culture supernatant, consistent with the role of LpHo as a pore-forming protein and L. plantarum ghost formation. The holin-induced L. plantarum BG platform could be developed as a safer alternative vehicle for the delivery of biomolecules. [ABSTRACT FROM AUTHOR]
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- 2023
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46. Computational Simulation of Holin S105 in Membrane Bilayer and Its Dimerization Through a Helix-Turn-Helix Motif
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Yinghao Wu, Brian Zhou, and Zhaoqian Su
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0303 health sciences ,Physiology ,Chemistry ,030310 physiology ,Bilayer ,Biophysics ,Cell Biology ,Bacteriophage lambda ,Turn (biochemistry) ,Viral Proteins ,03 medical and health sciences ,Transmembrane domain ,Membrane protein ,Holin ,Helix ,Amino Acid Sequence ,Lipid bilayer ,Dimerization ,Alpha helix ,Helix-Turn-Helix Motifs ,030304 developmental biology - Abstract
During the final step of the bacteriophage infection cycle, the cytoplasmic membrane of host cells is disrupted by small membrane proteins called holins. The function of holins in cell lysis is carried out by forming a highly ordered structure called lethal lesion, in which the accumulation of holins in the cytoplasmic membrane leads to the sudden opening of a hole in the middle of this oligomer. Previous studies showed that dimerization of holins is a necessary step to induce their higher order assembly. However, the molecular mechanism underlying the holin-mediated lesion formation is not well understood. In order to elucidate the functions of holin, we first computationally constructed a structural model for our testing system: the holin S105 from bacteriophage lambda. All atom molecular dynamic simulations were further applied to refine its structure and study its dynamics as well as interaction in lipid bilayer. Additional simulations on association between two holins provide supportive evidence to the argument that the C-terminal region of holin plays a critical role in regulating the dimerization. In detail, we found that the adhesion of specific nonpolar residues in transmembrane domain 3 (TMD3) in a polar environment serves as the driven force of dimerization. Our study therefore brings insights to the design of binding interfaces between holins, which can be potentially used to modulate the dynamics of lesion formation.
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- 2021
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47. Getting Outside the Cell: Versatile Holin Strategies Used by Distinct Phages to Leave Their Bacillus thuringiensis Host
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Audrey Leprince, Manon Nuytten, Elise July, Coralie Tesseur, Jacques Mahillon, and UCL - SST/ELI/ELIM - Applied Microbiology
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bacteriophages ,Host Microbial Interactions ,bacterial lysis ,Immunology ,Bacillus thuringiensis ,Membrane Proteins ,Bacillus Phages ,Microbiology ,Virology ,Insect Science ,endolysins ,Endopeptidases ,Bacillus cereus group ,Escherichia coli ,holin - Abstract
Holins are small transmembrane proteins involved in the final stage of the lytic cycle of double-stranded DNA (dsDNA) phages. They cooperate with endolysins to achieve bacterial lysis, thereby releasing the phage progeny into the extracellular environment. Besides their role as membrane permeabilizers, allowing endolysin transfer and/or activation, holins also regulate the lysis timing. In this work, we provide functional characterization of the holins encoded by three phages targeting the Bacillus cereus group. The siphovirus Deep-Purple has a lysis cassette in which holP30 and holP33 encode two proteins displaying holin properties, including a transmembrane domain. The holin genes were expressed in Escherichia coli and induced bacterial lysis, with HolP30 being more toxic than HolP33. In Bacillus thuringiensis, the simultaneous expression of both holins was necessary to observe lysis, suggesting that they may interact to form functional pores. The myoviruses Deep-Blue and Vp4 both encode a single candidate holin (HolB and HolV, respectively) with two transmembrane domains, whose genes are not located near the endolysin genes. Their function as holin proteins was confirmed as their expression in E. coli impaired cell growth and viability. The HolV expression in B. thuringiensis also led to bacterial lysis, which was enhanced by coexpressing the holin with its cognate endolysin. Despite similar organizations and predicted topologies, truncated mutants of the HolB and HolV proteins showed different toxicity levels, suggesting that differences in amino acid composition influence their lysis properties.
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- 2022
48. Bacteriophage-encoded protein utilization in bacterial ghost production: a mini-review
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Xuan, Guanhua, Qiu, Dongdong, Wang, Yinfeng, Wang, Jingxue, and Lin, Hong
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- 2024
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49. Biological Characterization and Evolution of Bacteriophage T7-△holin During the Serial Passage Process.
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Xu, Hai, Bao, Xi, Hong, Weiming, Wang, Anping, Wang, Kaimin, Dong, Hongyan, Hou, Jibo, Govinden, Roshini, Deng, Bihua, and Chenia, Hafizah Y.
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BIOLOGICAL evolution ,DELETION mutation ,NUCLEOTIDE sequencing ,TRANSMISSION electron microscopy ,GENETIC mutation - Abstract
Bacteriophage T7 gene 17.5 coding for the only known holin is one of the components of its lysis system, but the holin activity in T7 is more complex than a single gene, and evidence points to the existence of additional T7 genes with holin activity. In this study, a T7 phage with a gene 17.5 deletion (T7-△holin) was rescued and its biological characteristics and effect on cell lysis were determined. Furthermore, the genomic evolution of mutant phage T7-△holin during serial passage was assessed by whole-genome sequencing analysis. It was observed that deletion of gene 17.5 from phage T7 delays lysis time and enlarges the phage burst size; however, this biological characteristic recovered to normal lysis levels during serial passage. Scanning electron microscopy showed that the two opposite ends of E. coli BL21 cells swell post-T7-△holin infection rather than drilling holes on cell membrane when compared with T7 wild-type infection. No visible progeny phage particle accumulation was observed inside the E. coli BL21 cells by transmission electron microscopy. Following serial passage of T7-△holin from the 1st to 20th generations, the mRNA levels of gene 3.5 and gene 19.5 were upregulated and several mutation sites were discovered, especially two missense mutations in gene 19.5 , which indicate a potential contribution to the evolution of the T7-△holin. Although the burst size of T7-△holin increased, high titer cultivation of T7-△holin was not achieved by optimizing the culture process. Accordingly, these results suggest that gene 19.5 is a potential lysis-related component that needs to be studied further and that the T7-△holin strain with its gene 17.5 deletion is not adequate to establish the high-titer phage cultivation process. [ABSTRACT FROM AUTHOR]
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- 2021
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- View/download PDF
50. First joint oscillation analysis of Super-Kamiokande atmospheric and T2K accelerator neutrino data
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Super-Kamiokande, collaborations, T2K, Abe, S., Abe, K., Akhlaq, N., Akutsu, R., Alarakia-Charles, H., Ali, A., Hakim, Y. I. Alj, Monsalve, S. Alonso, Amanai, S., Andreopoulos, C., Anthony, L. H. V., Antonova, M., Aoki, S., Apte, K. A., Arai, T., Arihara, T., Arimoto, S., Asada, Y., Asaka, R., Ashida, Y., Atkin, E. T., Babu, N., Barbi, M., Barker, G. J., Barr, G., Barrow, D., Bates, P., Batkiewicz-Kwasniak, M., Beauchêne, A., Berardi, V., Berns, L., Bhadra, S., Bhuiyan, N., Bian, J., Blanchet, A., Blondel, A., Bodur, B., Bolognesi, S., Bordoni, S., Boyd, S. B., Bravar, A., Bronner, C., Bubak, A., Avanzini, M. Buizza, Burton, G. T., Caballero, J. A., Calabria, N. F., Cao, S., Carabadjac, D., Carter, A. J., Cartwright, S. L., Casado, M. P., Catanesi, M. G., Cervera, A., Chakrani, J., Chalumeau, A., Chen, S., Cherdack, D., Choi, K., Chong, P. S., Chvirova, A., Cicerchia, M., Coleman, J., Collazuol, G., Cook, L., Cormier, F., Cudd, A., Dalmazzone, C., Daret, T., Dasgupta, P., Davis, C., Davydov, Yu. I., De Roeck, A., De Rosa, G., Dealtry, T., Delogu, C. C., Densham, C., Dergacheva, A., Dharmapal, R., Di Lodovico, F., Lopez, G. Diaz, Dolan, S., Douqa, D., Doyle, T. A., Drapier, O., Duffy, K. E., Dumarchez, J., Dunne, P., Dygnarowicz, K., D'ago, D., Edwards, R., Eguchi, A., Elias, J., Emery-Schrenk, S., Erofeev, G., Ershova, A., Eurin, G., Fannon, J. E. P., Fedorova, D., Fedotov, S., Feltre, M., Feng, J., Feng, L., Ferlewicz, D., Fernandez, P., Finch, A. J., Aguirre, G. A. Fiorentini, Fiorillo, G., Fitton, M. D., Patiño, J. M. Franco, Friend, M., Fujii, Y., Fujisawa, C., Fujita, S., Fukuda, Y., Furui, Y., Gao, J., Gaur, R., Giampaolo, A., Giannessi, L., Giganti, C., Glagolev, V., Goldsack, A., Gonin, M., Rosa, J. González, Goodman, E. A. G., Gorin, A., Gorshanov, K., Gousy-Leblanc, V., Grassi, M., Griskevich, N. J., Guigue, M., Hadley, D., Haigh, J. T., Han, S., Harada, M., Harris, D. A., Hartz, M., Hasegawa, T., Hassani, S., Hastings, N. C., Hayato, Y., Heitkamp, I., Henaff, D., Hill, J., Hino, Y., Hiraide, K., Hogan, M., Holeczek, J., Holin, A., Holvey, T., Van, N. T. Hong, Honjo, T., Horiuchi, S., Hosokawa, K., Hu, Z., Hu, J., Iacob, F., Ichikawa, A. K., Ieki, K., Ikeda, M., Iovine, N., Ishida, T., Ishino, H., Ishitsuka, M., Ishizuka, T., Ito, H., Itow, Y., Izmaylov, A., Izumiyama, S., Jakkapu, M., Jamieson, B., Jang, M. C., Jang, J. S., Jenkins, S. J., Jesús-Valls, C., Ji, J. Y., Jia, M., Jiang, J., Jonsson, P., Joshi, S., Jung, C. K., Jung, S., Kabirnezhad, M., Kaboth, A. C., Kajita, T., Kakuno, H., Kameda, J., Kanemura, Y., Kaneshima, R., Karpova, S., Kasetti, S. P., Kashiwagi, Y., Kasturi, V. S., Kataoka, Y., Katori, T., Kawamura, Y., Kawaue, M., Kearns, E., Khabibullin, M., Khotjantsev, A., Kikawa, T., Kim, S. 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- Subjects
High Energy Physics - Experiment - Abstract
The Super-Kamiokande and T2K collaborations present a joint measurement of neutrino oscillation parameters from their atmospheric and beam neutrino data. It uses a common interaction model for events overlapping in neutrino energy and correlated detector systematic uncertainties between the two datasets, which are found to be compatible. Using 3244.4 days of atmospheric data and a beam exposure of $19.7(16.3) \times 10^{20}$ protons on target in (anti)neutrino mode, the analysis finds a 1.9$\sigma$ exclusion of CP-conservation (defined as $J_{CP}=0$) and a preference for the normal mass ordering., Comment: 12 pages, 4 figures
- Published
- 2024
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